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牛睾丸酰基磷酸酶:纯化及氨基酸序列

Bovine testis acylphosphatase: purification and amino acid sequence.

作者信息

Pazzagli L, Cappugi G, Camici G, Manao G, Ramponi G

机构信息

Department of Biochemical Sciences, University of Florence, Italy.

出版信息

J Protein Chem. 1993 Oct;12(5):593-601. doi: 10.1007/BF01025124.

DOI:10.1007/BF01025124
PMID:8142002
Abstract

Two acylphosphatase molecular forms have been isolated from bovine testis. Their amino acid sequence was determined. One (ACY1) consists of 98 amino acid residues, while the other one (ACY2) consists of 100 amino acid residues. Both molecular forms are N-acetylated and differ only in the amino terminus. ACY2 has an additional Ser-Met tail with respect to ACY1. Both ACY1 and ACY2 are organ-common type isoenzymes and thus differ for about half of the amino acid positions from the previously sequenced bovine muscle isoenzyme.

摘要

已从牛睾丸中分离出两种酰基磷酸酶分子形式。测定了它们的氨基酸序列。一种(ACY1)由98个氨基酸残基组成,而另一种(ACY2)由100个氨基酸残基组成。两种分子形式均为N - 乙酰化,仅在氨基末端有所不同。相对于ACY1,ACY2有一个额外的丝氨酸 - 甲硫氨酸尾巴。ACY1和ACY2都是器官通用型同工酶,因此与先前测序的牛肌肉同工酶在大约一半的氨基酸位置上有所不同。

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A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure.
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