兔骨骼肌中副肌球蛋白的氨基酸序列。
Amino-acid sequence of parvalbumin from rabbit skeletal muscle.
作者信息
Enfield D L, Ericsson L H, Blum H E, Fischer E H, Neurath H
出版信息
Proc Natl Acad Sci U S A. 1975 Apr;72(4):1309-13. doi: 10.1073/pnas.72.4.1309.
Determination of the complete amino-acid sequence of rabbit skeletal muscle parvalbumin is described. The sequence of 86 of the 109 total residues was determined automatically by sequenator analyses of peptides obtained after cleavage with CNBr or with trypsin. The positions of the remaining 23 residues were determined by subtractive Edman degradation of tryptic and chymotryptic peptides. The protein has an acetylated amino terminus. Comparison of the rabbit parvalbumin with those from carp, hake, and pike and with the calcium binding subunit of rabbit muscle troponin indicates that these proteins are homologous. Among the parvalbumins a high degree of identity is observed, especially of residues involved in the binding of calcium or in the formation of the hydrophobic core.
本文描述了兔骨骼肌小清蛋白完整氨基酸序列的测定。通过对用溴化氰或胰蛋白酶裂解后得到的肽段进行序列分析仪分析，自动测定了109个总残基中86个残基的序列。其余23个残基的位置通过胰蛋白酶和糜蛋白酶肽段的减法埃德曼降解法确定。该蛋白质的氨基末端被乙酰化。将兔小清蛋白与鲤鱼、无须鳕和梭子鱼的小清蛋白以及兔肌肉肌钙蛋白的钙结合亚基进行比较，表明这些蛋白质是同源的。在小清蛋白中观察到高度的同一性，特别是在参与钙结合或疏水核心形成的残基方面。
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