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1
Structural studies on bovine -crystallin.
Biochem J. 1971 Feb;121(3):453-9. doi: 10.1042/bj1210453.
2
Amino acid sequences around the cysteine residue of calf lens -crystallin.
Biochem J. 1971 Aug;124(1):61-7. doi: 10.1042/bj1240061.
3
The amino acid sequence of -crystallin (fraction II) from calf lens.
Biochem J. 1972 Jul;128(4):961-70. doi: 10.1042/bj1280961.
4
The amino acid sequences of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin.
Biochem J. 1970 Feb;116(3):515-32. doi: 10.1042/bj1160515.
5
Structural studies on lens proteins.
Biochem J. 1967 Jul;104(1):128-34. doi: 10.1042/bj1040128.
6
Structural studies on calf lens gamma-crystallin fraction IV: a comparison of the cysteine-containing tryptic peptides with the corresponding amino acid sequence of gamma-crystallin fraction II.
Exp Eye Res. 1978 Mar;26(3):291-304. doi: 10.1016/0014-4835(78)90076-3.
7
Isolation of non-identical polypeptide chains of -crystallin.
Int J Protein Res. 1969;1(1):19-27. doi: 10.1111/j.1399-3011.1969.tb01623.x.
8
Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.
Biochem J. 1966 Oct;101(1):214-28. doi: 10.1042/bj1010214.
9
Microheterogeneity at the C-terminus of gamma-crystallin fraction IVb.
Biochem J. 1972 Apr;127(3):609-10. doi: 10.1042/bj1270609.
10
N-terminal sequences of alpha-crystallin.
Biochem J. 1969 Dec;115(4):789-96. doi: 10.1042/bj1150789.
引用本文的文献
1
C-terminal amino acid sequence of bovine -crystallin.
Biochem J. 1971 Feb;121(3):557-9. doi: 10.1042/bj1210557.
2
Microheterogeneity at the C-terminus of gamma-crystallin fraction IVb.
Biochem J. 1972 Apr;127(3):609-10. doi: 10.1042/bj1270609.
3
The amino acid sequence of -crystallin (fraction II) from calf lens.
Biochem J. 1972 Jul;128(4):961-70. doi: 10.1042/bj1280961.
4
Isolation of a zinc protein from the tapetum lucidum of the cat.
Biochem J. 1972 Nov;130(1):303-5. doi: 10.1042/bj1300303.
5
Modification of calf lens crystallins as determined by gel electrophoresis.
Mol Cell Biochem. 1976 Jul 30;12(1):9-14. doi: 10.1007/BF01731898.
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PREFERENTIAL RELEASE OF ASPARTIC ACID BY DILUTE ACID TREATMENT OF TRYPTIC PEPTIDES.
Biochemistry. 1965 May;4:793-801. doi: 10.1021/bi00881a001.
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HUMAN HEART CYTOCHROME C. CHYMOTRYPTIC PEPTIDES, TRYPTIC PEPTIDES, AND THE COMPLETE AMINO ACID SEQUENCE.
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[Amino acid determination on paper chromatograms].
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On the existence of an embryonic lens protein.
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The action of trypsin on polylysine.
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Structural studies on lens proteins.
Biochem J. 1967 Jul;104(1):128-34. doi: 10.1042/bj1040128.
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Separation of dansyl-amino acids by polyamide layer chromatography.
Biochim Biophys Acta. 1967 Feb 21;133(2):369-70. doi: 10.1016/0005-2795(67)90078-5.
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Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines.
Biochim Biophys Acta. 1966 Dec 28;130(2):538-40. doi: 10.1016/0304-4165(66)90256-x.
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Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.
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Study of the dansylation reaction of amino acids, peptides and proteins.
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