The denaturation of acetic acid-soluble calf-skin collagen. Changes in optical rotation, viscosity and susceptibility towards enzymes during serial denaturation in solutions of urea.
作者信息
STEVEN F S, TRISTRAM G R
出版信息
Biochem J. 1962 Oct;85(1):207-10. doi: 10.1042/bj0850207.
Abstract
摘要
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本文引用的文献
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THE EFFECTS OF PROTEASES ON THE TROPOCOLLAGEN MACROMOLECULE AND ON ITS AGGREGATION PROPERTIES.
Proc Natl Acad Sci U S A. 1960 Feb;46(2):197-206. doi: 10.1073/pnas.46.2.197.
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The presence of non-protein nitrogen in acetic acid-soluble calf-skin collagen.
Biochem J. 1962 May;83(2):240-4. doi: 10.1042/bj0830240.
3
The origin of N-terminal residues in acetic acid-soluble calf-skin collagen.
Biochem J. 1962 May;83(2):245-8. doi: 10.1042/bj0830245.
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The denaturation of ovalbumin. Changes in optical rotation, extinction and viscosity during serial denaturation in solutions of urea.
Biochem J. 1959 Sep;73(1):86-90. doi: 10.1042/bj0730086.
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[N-terminal and C-terminal residues of bovine chymotrypsinogen].
Biochim Biophys Acta. 1959 Mar;32(1):256-8. doi: 10.1016/0006-3002(59)90577-3.
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Structural changes in the activation of chymotrypsinogen and trypsinogen; effect of urea on chymotrypsinogen and delta-chymotrypsin.
Arch Biochem Biophys. 1956 Nov;65(1):243-59. doi: 10.1016/0003-9861(56)90191-6.
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Structure of collagen.
Nature. 1955 Sep 24;176(4482):593-5. doi: 10.1038/176593a0.
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