The denaturation of ovalbumin. Changes in optical rotation, extinction and viscosity during serial denaturation in solutions of urea.
作者信息
STEVEN F S, TRISTRAM G R
出版信息
Biochem J. 1959 Sep;73(1):86-90. doi: 10.1042/bj0730086.
Abstract
摘要
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引用本文的文献
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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.
Biochem J. 1962 Oct;85(1):207-10. doi: 10.1042/bj0850207.
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Studies of the denaturation and partial renaturation of ovalbumin.
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本文引用的文献
1
The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration.
Biochem J. 1943 Jul;37(2):302-10. doi: 10.1042/bj0370302.
2
The reactivity of free amino groups in native and denatured ovalbumin towards fluorodinitrobenzene.
Biochem J. 1958 Oct;70(2):179-82. doi: 10.1042/bj0700179.
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Liberation of tyrosine hydroxyl groups in urea solutions of bovine serum albumin and ovalbumin.
Nature. 1957 Dec 7;180(4597):1286-7. doi: 10.1038/1801286a0.
4
Protein structure in relation to function and biosynthesis.
Adv Protein Chem. 1956;11:1-100. doi: 10.1016/s0065-3233(08)60420-9.
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