Korean J Dermatol.  1976 Jun;14(2):115-121.

Studies of Enzymes in Hyman Skin Tissue

• Kim YP
• Kahng JB

Abstract

Gamma-glutamyl transpeptidase (GGTP) activity was measured in the homogenate of penile foreskin, using y-glutamyl-p-nitroanilide, as a substrate, and it was found that (GGTP) activity was present in the epidermis and dermis, being more active in the former. The optimum pH for the enzyme was 8.5 - 9.0 in Tris buffer, which was similar to those of the rat kidney and human serum enzymes. It was also revealed that glycylglycine was the most effective activator of the enzyme and some activation was also observed in the presence of L-glutamine. But L-rnethionine, L-homoserine, L-glutamic acid, L-arginine, L-aspartic acid, glycine and L-valine inhibited the activity, suggesting that these amino acids do not act as acceptors of p-glutamyl moiety. The enzyme was remarkably inhibited by bromosulphalein, oxidised gluta,thione, and by L-serine in the presence of borate, and the inhibitions were more severe than is the case with the rat kidney and human serum enzymes.

MeSH Terms

Amino Acids
Animals
Arginine
Aspartic Acid
Dermis
Epidermis
Foreskin
gamma-Glutamyltransferase
Glutamic Acid
Glutamine
Glycine
Glycylglycine
Humans
Hydrogen-Ion Concentration
Kidney
Patient Acceptance of Health Care
Rats
Serine
Skin*
Tromethamine
Valine
Amino Acids
Arginine
Aspartic Acid
Glutamic Acid
Glutamine
Glycine
Glycylglycine
Serine
Tromethamine
Valine
gamma-Glutamyltransferase