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Molecular Cloning and Expression of Biologically Active Human Glia Maturation Factor‐β
Author(s) -
Kaplan Ruth,
Zaheer Asgar,
Jaye Michael,
Lim Ramon
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb03777.x
Subject(s) - biology , complementary dna , cloning (programming) , recombinant dna , molecular cloning , escherichia coli , cdna library , amino acid , microbiology and biotechnology , clone (java method) , peptide sequence , signal peptide , biochemistry , gene , computer science , programming language
Glia maturation factor‐β, a protein found in the brains of all vertebrates thus far examined, appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. Using oligonucleotide probes based on the sequences of three tryptic peptides derived from bovine glia maturation factor‐β, we screened a human brainstem cDNA library in δll. A 0.7‐kb clone was isolated, sequenced in its entirety, and found to encode a polypeptide of 142 amino acids which contained regions identical to the three bovine peptides. This polypeptide, human recombinant glia maturation factor‐β, has been expressed in Escherichia coli and found to possess structural characteristics and biological activity indistinguishable from those of the native bovine protein.