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Volume 74 (1973)
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- Issue 2 Pages 203-
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Volume 74, Issue 2
Displaying 1-24 of 24 articles from this issue
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Hiroshi HAYASHI1973 Volume 74 Issue 2 Pages 203-208
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA leucine transfer ribonucleic acid was coupled to Sepharose 4B after activation of the Sepharose beads with cyanogen bromide. Affinity chromatography was performed on the tRNA conjugate of Sepharose. The matrix, besides the enzyme, retained considerable amounts of other proteins. The specificity of the matrix, therefore, was not as strict as was expected from the specificity of the aminoacylating reaction. The nature of the non-specific adsorption is discussed. A specific purification of leucyl-tRNA synthetase (75-fold), however, was accomplished by choosing suitable conditions for the eluting step, i. e., the pH and salt concentration. The method elaborated is one of the most effective procedures for the purification of the enzyme.View full abstractDownload PDF (411K) -
Hideo MOHRI, Masako SHIMOMURA1973 Volume 74 Issue 2 Pages 209-220
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTubulin (microtubule protein) and actin were isolated from sea-urchin sperm flagella and lantern muscle, respectively, and their physicochemical properties were compared.
Although somewhat similar, they differed in size, amino acid composition, and molecular weight. Their peptide maps, obtained by digestion with either trypsin [EC 3. 4. 4. 4] or pronase were also different. Activation of myosin ATPase [EC 3. 6. 1. 3] at low ionic strength and decrease in viscosity on adding ATP at high ionic strength are criteria for identifying an unknown protein as actin. These phenomena were not observed with tubulin, even when microtubules were prepared from flagella without treatment with digitonin, Triton X-100 or EDTA. However, tubulin co-precipitated with myosin in the presence of ATP to some extent.
These results support our previous conclusion that tubulin and actin are different proteins.View full abstractDownload PDF (4831K) -
Kiyoshi IKEDA, Kozo HAMAGUCHI1973 Volume 74 Issue 2 Pages 221-230
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSCharge transfer binding of N1-methylnicotinamide chloride to tryptophan derivatives and to Trp 62 of hen egg-white lysozyme [EC 3. 2. 1. 17] was studied by the circular dichroic technique. The data for tryptophan derivatives at various pH's and ionic strengths suggested that electrostatic interaction between the positive charge of the pyridinium ion and charges located near the indole moiety was very important for the charge transfer interaction. Data on the pH dependence of the association constant for lysozyme, corrected for the electrostatic interaction, indicated that two ionizable groups having pK values of about 5.8 and 4.5 were perturbed slightly to lower values on charge transfer binding of N1-methylnicotinamide. The former group was assigned to the carboxyl group of Glu 35. This suggested that the state of Trp 62 is linked with the ionization of the catalytic carboxyl of Glu 35, which is spatially separated from Trp 62. It was also found that another ionizable group with a pK value of about 3.5 affects the molecular ellipticity of the complex.View full abstractDownload PDF (815K) -
II. Inactivation of Bovine Rennin by Acid Protease-Specific InhibitorsWen-Jong CHANG, Kenji TAKAHASHI1973 Volume 74 Issue 2 Pages 231-237
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Bovine rennin [EC 3. 4. 4. 3] was rapidly inactivated in 1 : 1 stoichiometry by reaction with diazoacetyl-DL-norleucine methyl ester (DAN) in the presence of cupric ions. It was also inactivated by reaction with l, 2-epoxy-3-(p-nitrophenoxy)propane (EPNP) with concomitant incorporation of two equivalents of the reagent into the enzyme. The DAN-inactivated enzyme and the EPNP-inactivated enzyme also reacted with EPNP and DAN, respectively, in the same way as native rennin. The reagent moieties incorporated into the enzyme were labilized by treatment with aqueous hydroxylamine. These results indicate the implication of two distinct carboxyl groups in these reactions, and hence in the active site of rennin.
2. Pepstatin, a specific inhibitor of pepsin [EC 3. 4. 4. 1], inhibited rennin over a wide pH range (pH 2.0-6.0). It also significantly inhibited the reactions with rennin of diazoacetyl-DL-norleucine methyl ester and 1, 2-epoxy-3-(p-nitrophenoxy) propane. These results indicate that pepstatin binds to at least part of the active site of rennin. p-Bromophenacyl bromide, a specific inactivator of pepsin, failed to inactivate rennin.View full abstractDownload PDF (589K) -
I. Isolation of Human Salivary KallikreinYukio FUJIMOTO, Hiroshi MORIYA, Chiaki MORIWAKI1973 Volume 74 Issue 2 Pages 239-246
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSHuman salivary kallikrein [EC 3. 4. 4. 21] was purified about 2, 200-fold with aa over-all yield of 35% by acetone precipitation, adsorption to DEAE-cellulose and hydroxyl-apatite gel, and column chromatographies on DEAE-Sephadex (A-50), Sephadex G-100, and Sephadex G-200.
The purified enzyme was homogeneous on disc and vertical plate polyacrylamide gel electrophoresis, ultracentrifugal analysis (sedimentation equilibrium method) and isoelectric focusing fractionation with carrier ampholytes. Its isoelectric point was 4.0, and the molecular weight was calculated to be about 28, 000 by gel nitration and 23, 500 by ultracentrifugation.View full abstractDownload PDF (496K) -
II. Properties of Purified Salivary KallikreinYukio FUJIMOTO, Chiaki MORIWAKI, Hiroshi MORIYA1973 Volume 74 Issue 2 Pages 247-252
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSPurified human salivary kallikrein [EC 3. 4. 4. 21] (HSK) caused a rapid release of kinin from bovine plasma kininogen, while it showed little proteolytic action on casein. Synthetic arginine esters, such as N-α-tosyl-L-arginine methyl ester (TAME) and N-α-benzoyl-L-arginine ethyl ester (BAEE), were good substrates for HSK, and the hydrolysis of TAME was faster than that of BAEE. The Km value towards BAEE was 4.1×10-4M and that for TAME was 5.7×10-4M. The pH optimum for TAME digestion was about 8 and this enzyme seemed to be rather heat-stable at this pH.
Effects of naturally occurring inhibitors, such as soy-bean trypsin inhibitor (SBTI), and Trasylol on the various activities of HSK were also studied. Trasylol strongly inhibited the three representative activities of HSK, but SBTI showed little inhibition on them.View full abstractDownload PDF (440K) -
II. Effects of Species and Concentration of AnionsToshihiko HAYASHI, Yutaka NAGAI1973 Volume 74 Issue 2 Pages 253-262
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe relationship between the rate of collagen fibril formation and the concentration of various anions has been examined. Collagen fibril formation by pepsin-treated collagen depends strongly on the concentration of divalent anions, but only slightly on that of monovalent anions. Addition of glucose or urea, an inhibitor of collagen fibril formation, increased the dependency of fibril formation on phosphate (divalent) concentration, while addition of SDS, a promoter of collagen fibril formation, reduced it. The dependency of fibril formation on phosphate concentration was increased, as the incubation temperature was lowered. A reduced dependency of collagen fibril formation on phosphate concentration was observed with acid-soluble collagen, suggesting that the non-helical regions of collagen molecules participate in the molecular interactions. However, addition of glucose caused acid-soluble collagen to behave in a similar way to the pepsin-treated material in this respect, indicating that the molecular interactions of collagen depend essentially on phosphate concentration. Redissolution of fibrils formed in vitro proceeded faster with pepsin-treated collagen than with the acid-soluble material. The effects of various factors on collagen fibril formation are discussed in relation to the hypothesis that water structure is crucial in collagen fibril formation.View full abstractDownload PDF (775K) -
I. Characterization of the ReactionYo'ichiro MITSUNARI, Katsuji HORI1973 Volume 74 Issue 2 Pages 263-271
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe general properties of Qβ replicase-associated, polycytidylic acid-dependent polyguanylic acid polymerase (poly (G) polymerase) have been investigated. The results indicated that the poly (G) polymerase reaction was distinct from the Qβ replicase reaction by several different criteria: (1) Optimum temperature of the poly (G) polymerase reaction was 28-32°C, whereas that of the Qβ replicase reaction was 32-35°C. (2) Mn2+ could entirely substitute for Mg2+ in the poly (G) polymerase reaction, but could not do so in the Qβ replicase reaction. (3) The Km for GTP of the poly (G) polymerase was 2×lO-5M, which was about one-tenth of that for GTP of the Qβ replicase. (4) The poly (G) polymerase catalyzed the synthesis of poly (G) by transcribing poly (C), but did not catalyze the further reaction: synthesis of poly (C) from poly (G).View full abstractDownload PDF (708K) -
II. Effect of Natural and Synthetic Polyribonucleotides on the ReactionKatsuji HORI1973 Volume 74 Issue 2 Pages 273-278
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe effects of natural and synthetic polyribonucleotides on both the polycytidylic acid-dependent polyguanylic acid polymerase (poly (G) polymerase) and Qβ replicase reactions have been investigated. Among the polymers examined, poly (U) and Qβ RNA strongly inhibited the poly (G) polymerase, but f2 RNA, E. coli tRNA, poly (A) did not. Poly (U) was found to compete with poly (C) for the enzyme, while Qβ RNA did not compete with poly (C), but reduced the Vmax, suggesting that Qβ RNA affects the poly (G) polymerase activity noncompetitively.
Inhibition by Qβ RNA of the poly (G) polymerase was restored by the addition of HFI. The degree of recovery depended upon the ratio of HFI to Qβ RNA. Complete restoration of the poly (G) polymerase activity was attained at a molar ratio of 2 to 10 HFI molecules per molecule of Qβ RNA.
Poly (C) was found to inhibit the Qβ replicase activity noncompetitively. Similar but somewhat less strong inhibition occurred on the addition of poly (U), poly (A), poly (A+2U), and poly (I).
Following kinetic studies, it was concluded that the poly (C) binding site was not identical with that of Qβ RNA.View full abstractDownload PDF (433K) -
Kozo ISHIDATE, Michinao MIZUGAKI, Mitsuru UCHIYAMA1973 Volume 74 Issue 2 Pages 279-283
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSCandida cells efficiently catalyzed the hydrogenation of 5-hydroxyundec-cis-2-enoic acid. The resulting saturated compound underwent further β-oxidation. Preparations from the 105, 000×g supernatant fraction of cell-free extracts of Candida also catalyzed the reduction of 5-hydroxyundec-cis-2-enoyl and oct-cis-2-enoyl Coenzyme A derivatives in the presence of NADPH as a specific electron donor. This reduction of cis-2-enoates may generally accompany the β-oxidation of unsaturated fatty acids.View full abstractDownload PDF (404K) -
Yoshio UENO, Michiko NAKAJIMA, Kosei SAKAI, Kenji ISHII, Norio SATO, N ...1973 Volume 74 Issue 2 Pages 285-296
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe inhibitory effects of fourteen kinds of 12-13-epoxy trichothec mycotoxins and related antibiotics on protein and DMA syntheses in reticulocytes, Ehrlich ascites tumor cells, rat liver and bacteria were investigated in whole-cell and cell-free systems, and the following results were obtained;
1. Among the fourteen compounds tested, twelve trichothecenes inhibited the uptake of 14C-leucine by whole cells of rabbit reticulocytes. The inhibitory effect varied over a wide range on chemical modification of the side chain and double bond.
2. In Ehrlich ascites tumor cells, the mycotoxins inhibited the uptake of 14C-leucine and 14-thymidine without affecting that of 14C-uracil.
3. When rabbit reticulocytes were treated with low concentrations of the tricho-thecenes, a marked degradation of polyribosomes was observed.
4. In cell-free systems of reticulocytes and rat liver, the trichothecenes inhibited the poly-U-dependent synthesis of polyphenylalanine in concentrations lower than the inhibitory concentrations of puromycin and cycloheximide, and the concentrations of various trichothecenes required for 50% inhibition were correlated with their lethal doses in mice.
5. In whole-cell and cell-free systems of Escherichia coli, fusarenon-X did not inhibit protein synthesis. A high concentration of the mycotoxin, slightly inhibited the uptake of 14C-amino acid in yeast (Geolrichum candidum).
6. Biochemical features of the actions of the trichothec mycotoxins were discussed in relation to their chemical and toxicological characteristics.View full abstractDownload PDF (792K) -
III. Enzymatic Properties of NAD-independent Glycerol-phosphate Dehydrogenase from Propionibacterium arabinosumNobuhito SONE1973 Volume 74 Issue 2 Pages 297-305
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSome enzymatic properties of the glycerol-phosphate dehydrogenase preparation from Propionibacterium arabinosum (1) are described.
1. The enzyme seemed to be specific for L-glycerol-3-phosphate and produced dihydroxyacetone phosphate in the presence of a suitable electron acceptor. DCIP, PMS, and ferricyanide were good electron acceptors. Molecular oxygen was a poor electron acceptor with concomitant production of H2O2.
2. The optimum pH for glycerol-P oxidation with DCIP was found to be 7.4 and Km for L-glycerol-3-P, to be 2.6×10-5M.
3. Sulfhydryl-binding reagent PCMB inhibited the enzyme activity and a limited inhibition was observed upon addition of amytal, dicumarol, dipyridyl, and thenoyl-trifluoroacetone. Hydrogen peroxide seemed to inactivate the enzyme.
4. Flavin, non-heme iron, and menaquinone were involved in the dehydrogenase preparation. Participation of menaquinone in the activity was confirmed by depletion-restoration experiments.
5. These characteristics of glycerol-P dehydrogenase were compared with those of the enzymes from other sources.View full abstractDownload PDF (644K) -
Tadahiko FUJII, Kuniko KOBAYASHI1973 Volume 74 Issue 2 Pages 307-311
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Steer hide collagen was solubilized by pronase (Streptomyces protease) at the highest rate at pH 6.0 in the presence of CaCl2. On raising the pH, the rate of solubilization of the collagen decreased markedly, though the specific activity of pronase increased.
2. The rate of solubilization of collagen reduced with sodium borohydride was very low compared to that of native collagen.
3. Kinetic analysis of the solubilization process indicated that the high solubilization rate at pH 6.0 is due to the dissociation of intermolecular cross-links of a Schiff base type in collagen fibers and to the pH dependence of pronase activity.View full abstractDownload PDF (411K) -
I. Complete Digestion with Pancreatic Ribonuclease and Ribonuclease T1Shosuke TAKEMURA, Kazuko OGAWA, Kotoe NAKAZAWA1973 Volume 74 Issue 2 Pages 313-322
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAlanine tRNA from Torulopsis utilis was highly purified by a series of DEAE-Sephadex column chromatographic procedures. The purified tRNA was completely digested with pancreatic ribonuclease and with ribonuclease T1. The end-products were isolated by column chromatography and their nucleotide sequences were determined by column, paper or thin-layer chromatographic procedures. The results of analyses of the two digests indicate that this tRNA is composed of 76 nucleotide residues, including 13 modified nucleotides. This tRNA differs in 8 nucleotides from, and lacks 2 nucleotides of, Saccharomyces tRNAAla. The complete sequence of this tRNA has been established after partial digestion with ribonuclease T1, as described in the subsequent paper.View full abstractDownload PDF (765K) -
II. Partial Digestion with Ribonuclease T1 and Derivation of the Complete SequenceShosuke TAKEMURA, Kazuko OGAWA1973 Volume 74 Issue 2 Pages 323-333
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSPartial RNase T1 [EC 2. 7. 7. 26] digestion of tRNAla1 (Torulopsis utilis) in the presence of Mg2+ yielded two half molecules by scission at the anticodon site. Several large oligonucleotides smaller than the halves were obtained by partial RNase T1 digestion of the tRNA in the absence of Mg2+. The sequences of these large fragments were analyzed. The complete sequence of this tRNA was derived from the results of these analyses and those described in the preceding paper. The cloverleaf model for the secondary structure was compared with that of Saccharomyces tRNAAla, as regards the aminoacyl-tRNA synthetase recognition sites.View full abstractDownload PDF (772K) -
Teruo IWASAKI, Toshifumi KIYOHARA, Mitsuyoshi YOSHIKAWA1973 Volume 74 Issue 2 Pages 335-340
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA single peptide bond of potato proteinase inhibitor II-b is selectively split by a catalytic quantity of TLCK-treated bovine chymotrypsin [EC 3. 4. 4. 5] at pH 3. Fragmentation of the chymotrypsin-modified inhibitor by reduction and S-carboxymeth-ylation, followed by gel nitration through Sephadex G-50, reveals that the specific peptide bond cleaved is the Lys-Ser bond of residues 63 and 64 in the inhibitor molecule. The modified inhibitor retains the full activity of native inhibitor Il-b. However, it shows decreased activities against bovine chymotrypsin and a bacterial proteinase, Nagarse, on elimination of the newly formed carboxyl-terminal lysine from the molecule. The losses of activities against the two enzymes almost parallel the extent of removal of lysine. Therefore, it is concluded that the Lys-Ser bond of residues 63 and 64 in inhibitor II-b is the main reactive site of the inhibitor for both chymotrypsin and Nagarse.View full abstractDownload PDF (452K) -
On the Heterologous Mischarging by Yeast Phenylalanyl-tRNA SynthetaseS. Anand KUMAR, Manuel KRAUSKOPF, James OFENGAND1973 Volume 74 Issue 2 Pages 341-353
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe ability of yeast phenylalanyl-tRNA synthetase to carry out the heterologous mischarging of nine E. coli tRNAs with phenylalanine, and the presence of a common sequence in these tRNAs in the double stranded region adjacent to the dihydrouridine loop, has led to the proposal (by Dudock) that this region of the tRNA is involved in recognition by the yeast enzyme. The validity of this hypothesis has now been examined by chemical modification of the region in question using as a test tRNA, E. coli tRNAVal1.
Photochemical cross-linking of 4S(8) and C(13) by irradiation at 335nm led to a complete loss of the ability of yeast phenylalanyl-tRNA synthetase to functionally recognize tRNAVal1 and the rate of cross-linking was correlated with the rate of loss of activity when appropriate assay conditions were used. Cross-linking had no effect on the recognition by the homologous E. coli valyl-tRNA synthetase [EC 6. 1. 1. 9].
Similarly, S-alkylation of the 4S(8) residue with iodoacetamide at pH 9 yielded the uridine-4-thio (2-acetamide) derivative of tRNA with no loss of homologous recognition but with complete loss of heterologous charging activity.
These results provide evidence that at least part of the yeast phenylalanyl-tRNA synthetase recognition site is located in the region of the tRNA proposed by Dudock, and, as a corollary, show that the E. coli valyl-tRNA synthetase recognition site(s) must be elsewhere in the molecule.View full abstractDownload PDF (1092K) -
Isolation and Characterization of Two Closely Related Components, SB1 and SB2Noriko TAKAHASHI, Yoko YASUDA, Kashiko GOTO, Tokiko MIYAKE, Takashi MU ...1973 Volume 74 Issue 2 Pages 355-373
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSStem bromelain [EC 3. 4. 4. 24] preparation which had been purified by the conventional method and hitherto found to be apparently homogeneous [T. Murachi, M. Yasui, and Y. Yasuda, Biochemistry, 3, 48 (1964)] was subjected to further fractionation on SE- or (SP-) Sephadex C-50 under well-defined conditions. A reproducible elution profile indicated a multiplicity of components. The two most abundant components, SB1 and SB2, in that order, were isolated by rechromatography as distinct entities. Components SB1 and SB2 were found to be indistinguishable on the basis of molecular weight determinations by ultracentrifugation, polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, immunoelectrophoresis, carbohydrate composition, and catalytic properties toward casein as well as toward synthetic ester substrates. SB1 and SB2 have an identical amino-terminal sequence, Val-Pro-Gln-, and an identical carboxyl end-group, glycine. The amino acid sequence around the reactive cysteinyl residue (CYS-) of SB1 was determined to be:
Ser-Val-Lys-Asn-Gln-Asn-Pro-Cys-Gly-Ala-CYS-Trp_??_Gly-Cys-Lys
An identical octapeptide sequence, italicized above, was found for SB2. The amino acid composition of SB1 was almost identical with that of SB2 except for only a few residues per molecule of m. w. 28, 000. Very similar tryptic peptide maps were obtained from SB1 and SB2, with only a few points of variance. It is concluded that SB1 and SB2 are very similar but not entirely identical components.View full abstractDownload PDF (1506K) -
Kazuko HORI, Takashi HASHIMOTO, Mitsuhiro NOZAKI1973 Volume 74 Issue 2 Pages 375-384
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSKinetic studies were carried out with nonheme iron containing dioxygenases, metapyrocatechase [EC 1. 13. 1. 2], and protocatechuate 3, 4-dioxygenase [EC 1. 13. 1. 3]. Both enzymes catalyze the cleavage of a catechol ring with insertion of two atoms of molecular oxygen, although the former contains a ferrous form of iron and the latter a ferric form.
Initial velocity plots with one substrate as the fixed substrate and the other as the variable substrate gave intersecting patterns of lines for both enzymes, indicating that a ternary complex of the enzyme with oxygen and an organic substrate is involved in these dioxygenase-catalyzed reactions. o-Nitrophenol and m-phenanthroline, dead end inhibitors for metapyrocatechase, each inhibited the enzyme competitively with respect to the organic substrate, catechol, and noncompetitively with respect to the other substrate, molecular oxygen. Likewise, a dead end inhibitor for protocatechuate 3, 4-dioxygenase, protocatechualdehyde, which is a structural analogue of the organic substrate, inhibited this enzyme competitively with respect to protocatechuic acid and noncompetitively with respect to oxygen.
These results are consistent with an ordered Bi Uni mechanism where an organic substrate first combines with the enzyme, and then reacts with oxygen to form a ternary complex. In product inhibition studies with metapyrocatechase, parabolic noncompetitive patterns were observed with respect to either substrate, and no significant product inhibition was observed with protocatechuate 3, 4-dioxygenase. Therefore, a rapid equilibrium random mechanism can not be completely ruled out.View full abstractDownload PDF (738K) -
Tetsu HOZUMI, Katsuhisa TAWADA1973 Volume 74 Issue 2 Pages 385-387
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
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Keiichi YOSHIMURA1973 Volume 74 Issue 2 Pages 389-391
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
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Hidenori HAYASHI, Tetsuya SUGA, Shinkichi NIINOBE1973 Volume 74 Issue 2 Pages 393-395
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (205K) -
Keitaro HIROMI, Masatake OHNISHI, Susumu SHIBATA1973 Volume 74 Issue 2 Pages 397-400
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
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Shigeharu NAGASAWA, Toshiro NAKAYASU1973 Volume 74 Issue 2 Pages 401-403
Published: August 25, 1973
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (222K)
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