AMINO-ACID-SEQUENCE HOMOLOGY BETWEEN BOVINE AND HUMAN-PLATELET PROTEINS

被引:6
作者
CIAGLOWSKI, RE [1 ]
WALZ, DA [1 ]
机构
[1] WAYNE STATE UNIV, DEPT PHYSIOL, 540 E CANFIELD, DETROIT, MI 48201 USA
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1985年 / 82卷 / 04期
关键词
D O I
10.1016/0305-0491(85)90514-0
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 complete amino acid sequence of bovine platelet factor 4 (PF-4) was determined. Comparison of the 88 residue bovine protein with its 70 residue human counterpart indicated 73% homology. There is 53% homology between this bovine protein and another human platelet protein, beta-thromboglobulin (.beta.-TG). These heparin binding proteins share greatest homology around a lysine-rich octa-peptide near the carboxy-terminus which is the putative heparin binding domain. Graphic comparison of these proteins suggests that a point mutation at position 55 (human PF-4 numbering) could cause a significant difference among the folding properties of these 3 proteins and might be critical for their different heparin binding properties.
引用
收藏
页码:715 / 719
页数:5
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