PARVALBUMIN ISOFORMS IN CHICKEN MUSCLE AND THYMUS - AMINO-ACID-SEQUENCE ANALYSIS OF MUSCLE PARVALBUMIN BY TANDEM MASS-SPECTROMETRY

被引:31
作者
KUSTER, T
STAUDENMANN, W
HUGHES, GJ
HEIZMANN, CW
机构
[1] UNIV ZURICH,DEPT PEDIAT,DIV CLIN CHEM,CH-8032 ZURICH,SWITZERLAND
[2] UNIV GENEVA,MED CTR,DEPT BIOCHEM MED,CH-1211 GENEVA 4,SWITZERLAND
关键词
D O I
10.1021/bi00100a012
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
Parvalbumins are high-affinity Ca2+-binding proteins characterized by an EF-hand structure. Muscles of lower vertebrates contain up to five isoparvalbumins whereas higher vertebrates were believed to contain only one isoform per species. Recently Brewer et al. [Brewer, J. M., Wunderlich, J. K., & Ragland, W. (1990) Biochimie 72, 653-660] purified and sequenced a protein that they named avian thymic hormone, from chicken thymus. This protein, promoting immunological maturation of bone marrow cells in culture, was identified as a parvalbumin. The amino acid composition of this thymic parvalbumin was, however, considerably different from those of chicken muscle parvalbumin [Strehler, E. E., Eppenberger, H. M., & Heizman, C. W. (1977) FEBS Lett. 75, 127-133], suggesting the existence of two tissue-specific parvalbumins in chicken. We purified parvalbumin from chicken muscle, determined its complete amino acid sequence by tandem mass spectrometry, and showed that this protein is rather homologous to muscle parvalbumins from other species but different in 45 positions from the thymic parvalbumin. We discuss the possibility that a parvalbumin gene family might exist in higher vertebrates, expressed in a tissue-specific and developmentally regulated manner.
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页码:8812 / 8816
页数:5
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