MOLECULAR-CLONING AND CHARACTERIZATION OF AN ISOPRENYLATED 67 KDA PROTEIN

被引：22
作者：
ASUNDI, VK
STAHL, RC
SHOWALTER, L
CONNER, KJ
CAREY, DJ
机构：
[1] The Sigfried and Janet Weis Center for Research, Geisinger Clinic (26-13), Danville, PA 17822-2613
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1217卷 / 03期
关键词：
ISOPRENYLATION; 67 KDA PROTEIN; CDNA SEQUENCE; GENE EXPRESSION;
D O I：
10.1016/0167-4781(94)90284-4
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：
The cDNA coding for a 67 kDa protein (p67) was isolated from a rat Schwann cell library. A recombinant form of p67 expressed in bacteria was used to produce polyclonal anti-p67 antibodies. By immunoblot analysis p67 was found to be expressed in most tissues and cell lines examined. Inspection of the deduced amino acid sequence revealed a COOH-terminal consensus sequence for isoprenylation. Consistent with this finding, p67 was a substrate for isoprenylation in vitro by geranylgeranylpyrophosphate. p67 was associated predominantly with the particulate fraction of rat smooth muscle cells. The rat p67 sequence was highly homologous to a family of recently described human and mouse gamma-interferon inducible, guanine nucleotide binding proteins.
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收藏
页码：257 / 265
页数：9
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