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编码磷酸化酶激酶完整催化亚基的cDNA克隆的分离与序列分析

Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase.

作者信息

da Cruz e Silva E F, Cohen P T

出版信息

FEBS Lett. 1987 Aug 10;220(1):36-42. doi: 10.1016/0014-5793(87)80871-2.

DOI:10.1016/0014-5793(87)80871-2
PMID:3609320
Abstract

Synthetic oligonucleotides have been used to isolate a 1.85 kb clone containing the full length coding sequence for the catalytic subunit of rabbit skeletal muscle phosphorylase kinase from a cDNA library constructed in lambda gt10. Sequence analysis of the clone predicted an amino acid sequence in agreement with a published primary structure. Inspection of the codon usage revealed a strong preference for G or C nucleotides at the third codon position as found for several other skeletal muscle proteins. This cDNA clone should facilitate identification of functional domains, including the calmodulin-binding site, and investigation of the molecular basis of X-linked phosphorylase kinase deficiencies.

摘要

合成寡核苷酸已被用于从λgt10构建的cDNA文库中分离出一个1.85 kb的克隆,该克隆包含兔骨骼肌磷酸化酶激酶催化亚基的全长编码序列。对该克隆的序列分析预测的氨基酸序列与已发表的一级结构一致。对密码子使用情况的检查表明,与其他几种骨骼肌蛋白一样,在密码子的第三个位置强烈偏好G或C核苷酸。这个cDNA克隆应该有助于鉴定功能结构域,包括钙调蛋白结合位点,并有助于研究X连锁的磷酸化酶激酶缺陷的分子基础。

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