PRIMARY STRUCTURE OF CYTOCHROME C FROM SNAPPING TURTLE CHELYDRA SERPENTINA
PRIMARY STRUCTURE OF CYTOCHROME C FROM SNAPPING TURTLE CHELYDRA SERPENTINA
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DOI：
10.1021/bi00872a016
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发表时间：
1966-01-01
期刊：
影响因子：
2.9
通讯作者：
MARGOLIASH, E
中科院分区：
文献类型：
--
作者：
CHAN, SK;TULLOSS, I;MARGOLIASH, E
根据从胰凝乳蛋白酶消化物中分离的肽段的完整氨基酸序列，确定了鳄龟（Chelydra serpentina）心脏细胞色素c的一级结构。这些肽在整个序列中的位置通过与已知结构的其他15种细胞色素c的结构的同源性来分配。梭serpentina蛋白具有所有“Cystalian型”细胞色素的特征，包括疏水性和碱性残基的成簇分布、乙酰甘氨酸NH 2-末端残基、104个残基长的单链多肽链、在位置14和17处与半胱氨酰残基结合的血红素辅基以及在残基70-80处的典型不变序列Asn-Pro-Lys-Lys-Tyr-IIe-Pro-Gly-Thr-Met。位置33被天冬酰胺残基占据，与在其他细胞色素c中通常出现在该位置的组氨酰残基形成对比。这种取代的重要性进行了讨论，与最近的研究结果有关的性质，在细胞色素c的血红素形成集团。
The primary structure of the cytochrome c from hearts of the snapping turtle, Chelydra serpentina, has been determined from the complete amino acid sequences of peptides isolated from a chymotryptic digest. The positions of these peptides in the over-all sequence were assigned by homology to the structures of the other 15 cytochromes c of known structure. The C. serpentina protein bears the characteristics of all "mammalian-type" cytochromes c including the clustered distribution of hydrophobic and basic residues, an acetylglycine NH2-terminal residue, a single polypeptide chain 104 residues long, a heme prosthetic group bound to cysteinyl residues in positions 14 and 17, and the typical invariant sequence Asn-Pro-Lys-Lys-Tyr-IIe-Pro-Gly-Thr-Met at residues 70-80. Position 33 is occupied by an asparaginyl residue, as contrasted to the histidyl residue commonly occurring at this location in other cytochromes c. The importance of this substitution is discussed in connection with recent findings concerning the nature of the hemo-chrome-forming groups in cytochrome c.