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粗糙脉孢菌NADP特异性谷氨酸脱氢酶的氨基酸序列。胰蛋白酶肽段

The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides.

作者信息

Wootton J C, Taylor J G, Jackson A A, Chambers G K, Fincham J R

出版信息

Biochem J. 1975 Sep;149(3):739-48. doi: 10.1042/bj1490739.

DOI:10.1042/bj1490739
PMID:1000
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1165682/
Abstract

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.

摘要

用胰蛋白酶消化粗糙脉孢菌的NADP特异性谷氨酸脱氢酶，分离出了该多肽链452个残基中的441个残基组成的肽段，并对其进行了大致测序。更多实验细节已作为补充出版物SUP 50052（共11页）存放在英国西约克郡韦瑟比波士顿温泉市的大英图书馆（出借部），其地址为LS23 7BQ，可按照《生物化学杂志》（1975年）第145卷第5期所规定的条件从该处获取复印件。

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本文引用的文献

1
COMPLEMENTATION RELATIONSHIP OF NEUROSPORA AM MUTANTS IN RELATION TO THEIR FORMATION OF ABNORMAL VARIETIES OF GLUTAMATE DEHYDROGENASE.粗糙脉孢菌AM突变体在谷氨酸脱氢酶异常变体形成方面的互补关系。
Genet Res. 1965 Feb;6:121-9. doi: 10.1017/s0016672300003980.
2
A MUTANT ENZYME IN NEUROSPORA CRASSA INTERCONVERTIBLE BETWEEN ELECTROPHORETICALLY DISTINCT ACTIVE AND INACTIVE FORMS.粗糙脉孢菌中的一种突变酶，可在电泳上不同的活性和非活性形式之间相互转换。
J Mol Biol. 1964 Dec;10:423-37. doi: 10.1016/s0022-2836(64)80064-4.
3
Complementation at the am locus of Neurospora crassa: a reaction between different mutant forms of glutamate dehydrogenase.粗糙脉孢菌am位点的互补作用：谷氨酸脱氢酶不同突变形式之间的反应。
J Mol Biol. 1963 May;6:361-73. doi: 10.1016/s0022-2836(63)80049-2.
4
Genetically determined multiple forms of glutamic dehydrogenase in Neurospora crassa.粗糙脉孢菌中谷氨酸脱氢酶的遗传决定多种形式
J Mol Biol. 1962 Apr;4:257-74. doi: 10.1016/s0022-2836(62)80004-7.
5
Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.肽在纸上的电泳迁移率及其在酰胺基团测定中的应用。
Nature. 1966 Aug 6;211(5049):591-3. doi: 10.1038/211591a0.
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