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The primary structure of the parvalbumin II of pike (Esox lucius).

作者信息

Gerday C

出版信息

Eur J Biochem. 1976 Nov 1;70(1):305-18. doi: 10.1111/j.1432-1033.1976.tb10982.x.

DOI:10.1111/j.1432-1033.1976.tb10982.x
PMID:1009932
Abstract

The amino acid sequence of the parvalbumin II of the pike is reported. The protein has a molecular weight of 11 435. It consists of a single polypeptide chain of 107 amino acid residues with an acetyl group blocking the N-terminus and an alanine residue at the C-terminus. The molecule has been enzymically cleaved by trypsin, thermolysin and by the protease of the Staphylococcus aureus strain V8. Chemical cleavages make use of the CNBr reaction and of the sulfocyanoethylation method. The comparison of this amino acid sequence with that of the parvalbumin III of the pike indicates that these two homologous proteins belong respectively to two different subgroups derived from an early gene duplication of an ancestral gene at least prior to the differentiation of the Osteichthyes.

摘要

相似文献

1
The primary structure of the parvalbumin II of pike (Esox lucius).
Eur J Biochem. 1976 Nov 1;70(1):305-18. doi: 10.1111/j.1432-1033.1976.tb10982.x.
2
Amino-acid sequence of parvalbumin from rabbit skeletal muscle.兔骨骼肌中副肌球蛋白的氨基酸序列。
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引用本文的文献

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3
Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences.EF 手型钙调节蛋白的进化。I. 基于氨基酸序列的关系。
J Mol Evol. 1990 Jun;30(6):522-62. doi: 10.1007/BF02101108.
4
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Eur Biophys J. 1991;19(6):283-6. doi: 10.1007/BF00183316.