Primary structure of hemocyanin from Palinurus vulgaris

被引：12

作者：

Jekel, PA ^{[1
]}

Neuteboom, B ^{[1
]}

Beintema, JJ ^{[1
]}

机构：

[1] UNIV GRONINGEN,BIOCHEM LAB,NL-9747 AG GRONINGEN,NETHERLANDS

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1996年 / 115卷 / 02期

关键词：

amino acid sequence; evolutionary rate; hemocyanin; molecular evolution; Palinurus vulgaris; spiny lobsters; subunit heterogeneity;

D O I：

10.1016/0305-0491(96)00119-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The primary structure of hemocyanin from the spiny lobster Palinurus vulgaris was determined using a mixture of at least four slightly different subunits. Heterogeneities were observed in 32 (5%) of the positions. The amino acid sequence differs at about 20% of the positions from that of subunit a of Panulirus interruptus hemocyanin.

引用

页码：243 / 246

页数：4

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