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Volume 17 (1977)
- Issue 6 Pages 277-
- Issue 5 Pages 229-
- Issue 4 Pages 181-
- Issue 3 Pages 121-
- Issue 2 Pages 69-
- Issue 1 Pages 1-
Volume 17, Issue 4
Displaying 1-5 of 5 articles from this issue
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Masaru SOGAMI1977 Volume 17 Issue 4 Pages 181-195
Published: July 25, 1977
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSBecause of its ready availability and multiplicities of functions, such as its unusual and versatile liganding ability, plasma albumin has become one of the most extensively studied proteins. In the review, the author discussed on the following four items with relation to "THE DOMAIN MODEL" and the liganding ability of plasma albumin.
(1) Plasma albumin is considered microheterogeneous stemmed from studied of the N-F transition, a highly cooperative transition in acidic solution.
(2) As the pH of plasma albumin solution is lowered below the isoelectric point, plasma albumin shows three-step transitions, N-F1, F1-F2 transitions and acid-expansion.
(3) Near the physiological pH range (0.15M NaCl, 0.002M CaCl2: pH 7.0-8.0), plasma albumin shows the N-B transition, resulting in an increase of the conformational fluctuation.
(4) Above the neutral pH, the SH group of CYS34 of defatted plasma albumin catalyzes the intramolecular disulfide exchange reaction, resulting in the new isomeric form, A form.View full abstractDownload PDF (804K) -
Motowo TOMITA1977 Volume 17 Issue 4 Pages 196-204
Published: July 25, 1977
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSHuman erythrocyte membrane contains two glycoproteins as major components. One is called glycophorin A, which is composed of 131 amino acids and 16 oligosaccharide chains. Glycophorin A is organized into three distinct domains on the basis of the clustering of the amino acids of similar type. These include (1) a glycosylated segment, (2) a hydrophobic segment, and (3) carboxyl terminal segment which has an unusual concentration of hydrophilic amino acids. This unique structure is consistent with the suggestions that glycophorin A has a transmembrane structure. Glycophorin A may functions to keep the cell free in blood stream while this assumption has not been supported by any conclusive results yet. Another major glycoprotein is called band 3 protein, which is supposed to function as anion transport channel. The structural analyses of this glycoprotein are under progress at a number of laboratories. The two major glycoproteins which are also the major intrinsic membrane proteins appear to make intramembrane particle in the membrane.View full abstractDownload PDF (540K) -
Kazunori SUGIMOTO1977 Volume 17 Issue 4 Pages 205-213
Published: July 25, 1977
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSIn order to define the primary structure in promoter, two high level promoters contained in bacteriophage fd DNA have been sequenced. Comparison of two sequences however indicated that the longest sequence common to both was only TATAAT in the non-transcribed part of the region where RNA-polymerase forms a stable initiation complex. One of the promoters sequenced contained an R. Hha I cleavage site five base pairs upstream from the TATAAT sequence, and cleavage destroyed promoter function. This promoter was cleaved into two pieces at this site and DNA fragments derived from other regions were joined to the resulting fragments. Ligation of any fragment examined to the TATAAT-containing fragments restored promoter function. On the basis of these observations, the structure essential for the function of fd promoter is discussed.View full abstractDownload PDF (1044K) -
Akio IWASHIMA1977 Volume 17 Issue 4 Pages 214-218
Published: July 25, 1977
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSGeneral characteristics of the transport of several vitamins such as thiamine, riboflavin, pyridoxine and biotin in yeast are described.
These vitamins were taken up by resting yeast cells and retained against concentration gradients, and their transports were dependent on energy, pH, temperature and also displayed structural specificity and saturation kinetics.
It was shown that yeast cells contain, besides a specific system for the uptake of each vitamin, one for its efflux from the cells. The addition of vitamin such as thiamine, riboflavin, and biotin in the medium appeared to repress the synthesis of their transport components during growth. On the other hand, overshoot observed in the transports of pyridoxine and biotin was considered a fast regulatory mechanism by which cells prevent the accumulation of excessive vitamins.View full abstractDownload PDF (330K) -
[in Japanese]1977 Volume 17 Issue 4 Pages 219-224
Published: July 25, 1977
Released on J-STAGE: May 25, 2009
JOURNAL FREE ACCESSDownload PDF (403K)
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