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Volume 21, Issue 3
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Part IV. Fractionation and purification of conarachin I and IIKAZUHIRO YOTSUHASHI, KAZUO SHIBASAKI1974 Volume 21 Issue 3 Pages 111-115
Published: March 15, 1974
Released on J-STAGE: January 20, 2010
JOURNAL FREE ACCESSConarachin I and II were fractionated from conarachin fraction by gel filtration chromatography on a Sephadex G-200 column, and purified by re-gel filtration and by ion exchange chromatography on, a DEAE-Sephadex A-50 columm.
Conarachin I was heterogeneous from the results of gel electrophoresis and consisted of several different species of protein which had a sedimentation coeffcient of 1.7S on a 0.75% protein concentration, took no part in the association-dissociation reactions upon the changes of ionic strength at pH 8.6 and formed no subunit structure. The UV-spectrum showed a maximum at 274nm, E1%1cm=4.02.
Conarachin II was 7.8S and consisted of 2.1S subunits, and was associated into 13.0S form with the decrease of ionic strength, at pH 8.6 on a 0.72% protein concentration. No difference in mobilities between subunits on gel electrophoresis was observed. The UV-spectrum showed a maximum at 279nm, E1%1cm=7.25.View full abstractDownload PDF (856K) -
Part XII. Effect of pH and heating on the solubility of water extracted proteinKAZUYOSHI OKUBO, KAZUO SHIBASAKI1974 Volume 21 Issue 3 Pages 116-121
Published: March 15, 1974
Released on J-STAGE: January 20, 2010
JOURNAL FREE ACCESSThe effect of heating on the solubility of water extracted protein at various pH was studied; it was recognized that the minimum solubility near isoelectric point was decreased by heating and the diffrential solubility between unheating and heating was minimum at pH 6.0, but maximum between pH 6.5 and 8.5, and at pH 3.5. Also the effect of heating at various pH on the solubility against standard solvent (0.076M tris-citrate buffer, pH 8.6, containing 0.01M 2-mercaptoethanol) was studied; the solubility was decreased by heating over 70°C between pH 3 and 7, but the insolubilization by heating was not recognized below pH 3 and over 7.
The effect of heating at various pH on the gel electrophoretical behavior of the protein was studied; the main components, 7 and 11 S, were dissociated into the subunits by heating being followed polymerizing of the subunits, and the stability of the 11 S component against heating was higher over pH 9 and lower below pH 3 than the 7S component.View full abstractDownload PDF (323K) -
Part V. Molecular dimension and subunit structure of conarachin I and II.KAZUHIRO YOTSUHASHI, KAZUO SHIBASAKI1974 Volume 21 Issue 3 Pages 122-125
Published: March 15, 1974
Released on J-STAGE: January 20, 2010
JOURNAL FREE ACCESSConarachin I was heterogeneous and consisted of three kinds of main protein, which possessed glycine, threonine and serine(1:1:1)as the N-terminal amino acids (DNP method). The average molecular weight was 17, 000(1.8S)by sedimentation-diffusion method. The average axial ratio was estimated 2.9 from the frictional ratio f/f0=1.233 and 3.2 from the intrinsic viscosity [η]=0.043dl/g, assuming the molecule of a prolate ellipsoid of revolution with 30% hydration.
Conarachin II seemed to be consisted of five subunits having the average molecular weight of 38, 000, which possessed glycine, (iso-)leucine, aspartic acid and glutamic acid(2:1:1:1)as the N-terminal amino acids. The axial ratio of the monomer form(8.2S, M.W.180, 000)was estimated 5.5 from f/f0=1.442 and 5.6 from[η]=0.073dl/g, and the dimer form (13.3S, 370, 000) 5.4 from f/f0=1.433 and 5.1 from [η]=0.067dl/g.View full abstractDownload PDF (194K)
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