Purification of r-Glutamyltranspeptidase from Rat Primary Hepatoma Tissue and Preparation of a Tumor Associated Antigen
Yonsei Medical Journal
;
: 37-48, 1988.
Article
in English
| WPRIM
| ID: wpr-20078
ABSTRACT
r-Glutamyltranspeptidase (r-GT) from a rat hepatoma induced by 3'-methyl-4-dimethylaminoazobenzene (3'-Me DAB) was purified 833 fold. The purified enzyme had a specific activity of 15.0 U/mg protein with an overall yield of 3.8%. The molecular weight of native r-GT was estimated as about 350,000 daltons, whichs a multicomplex of a single polypetide having a M W of 59,000. Anti r-GT rabbit antiserum cross-reacted with kidney r-GT as well as liver r-GT. Tryptic digestion of r-GT followed by separation with Con A sepharose column chromatography resulted in two major glycopeptides. A tumor associated antigen was prepared by the conjugation of a tryptic glycopeptide of r-GT to keyhole limpets hemocyanin and an antibody against this antigen cross-reacted preferentially with r-GT in rat hepatoma tissue.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Gamma-Glutamyltransferase
/
Liver Neoplasms, Experimental
/
Animals
/
Molecular Weight
/
Antigens, Neoplasm
Limits:
Animals
Language:
English
Journal:
Yonsei Medical Journal
Year:
1988
Type:
Article
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