Abstract |
gamma-Glutamyl transpeptidase (gamma-GT) from human primary hepatoma was solubilised and purified 290-fold with 25% recovery. The kinetic and catalytic properties were compared with those purified from human fetal and normal adult liver. Hepatoma gamma-GT did not differ from the fetal and adult liver gamma-GT in its pH optima for transpeptidation and auto-transfer reaction, heat stability, Km for the two substrates and inhibition by L-serine + borate. Enzyme from the three sources behaved in a similar manner towards various cations, sulphhydryl reagents, amino acid dipeptides. Adult liver enzyme showed a 4 time higher Ki value for anthglutin than hepatoma and fetal liver. The hepatoma gamma-GT could not be differentiated from that of adult and fetal liver by concanavalin-A Sepharose 4B column chromatography. The tissue concentration of gamma-GT was 3 to 13 times higher in hepatoma and fetal liver than in adult liver.
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Authors | P Selvaraj, K A Balasubramanian, P G Hill |
Journal | Enzyme
(Enzyme)
Vol. 26
Issue 2
Pg. 57-63
( 1981)
ISSN: 0013-9432 [Print] Switzerland |
PMID | 6113139
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Glutamates
- gamma-Glutamyltransferase
- anthglutin
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Topics |
- Adult
- Aging
- Carcinoma, Hepatocellular
(enzymology)
- Drug Stability
- Female
- Glutamates
(pharmacology)
- Humans
- Kinetics
- Liver
(embryology, enzymology)
- Liver Neoplasms
(enzymology)
- Pregnancy
- gamma-Glutamyltransferase
(isolation & purification, metabolism)
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