Purification of recombinant pp60v-src protein tyrosine kinase and phosphorylation of peptides with different secondary structure preference.

Purification of recombinant pp60v-src protein tyrosine kinase and phosphorylation of peptides with different secondary structure preference.
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重组pp60v-src蛋白酪氨酸激酶的纯化和具有不同二级结构偏好的肽的磷酸化。

DOI:
10.1021/bi00449a013
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发表时间:
1989
期刊:
影响因子:
2.9
通讯作者:
Kaiser,ET
Kaiser,ET
中科院分区:
生物学3区
文献类型:
--
作者:
Radziejewski,C;Miller,WT;Mobashery,S;Goldberg,AR;Kaiser,ET

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Materials and MethodsProteins used as molecular weight markers were purchased from Pharmacia. ATP, raffinose, and galactose were obtained from the Sigma Chemical Co. Protease inhibitors were purchased from Boehringer Mannheim Biochemicals, p-Methylbenzhydrylamine and benzhydrylamine resins were Pierce products. All protected amino acids were purchased from Peninsula Laboratories Inc.[7-32P] ATP (3000 Ci/mmol) was supplied by NEN Research Products. 125I-Labeled goat anti-mouse antibodies were from NEN. Radioactive decay was measured by using an LKB 1219 Rackbeta liquid scintillation counter. Fission fragment ionization mass spec-trometric analysis was carried out at the Rockefeller UniversityBiotechnology Mass Spectrometry Research Resource. Amino acid analysis of the peptides was performed by using a Dionex amino acid analyzer according to the method of Moore and Stein (1963) after hydrolysis of the peptides in 6 N boiling HC1 at 110 C for 24 h. High-performance liquid chroma-
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