Work

Mechanism of ammoniagenesis in human kidney

Year: 1971

Type: article

Abstract: SOCIETYthe enzyme activity of the supernatant was raised threefold more than that of the pellet.The further addition of deoxycholate decreased the phosphate activation of glutaminase.This decrease was greater for the pellet enzyme than for the supernatant enzyme.The supernatant and pellet enzymes were then preincubated at elevated temperatures for various times.Preincubation at 600C for 10min almost completely destroyed the glutaminase activity of the pellet, but only slightly decreased the enzyme activity of the supernatant.In the presence of phosphate similar heat treatment almost completely destroyed the enzyme activity of both supernatant and pellet.These results indicate that the enzyme which is released in the supernatant is different from that which remains in the pellet.

Source: Biochemical Journal

DOI: 10.1042/bj1250094pa

Authors: E Bourke, A Fine, J Scott

Institution: Trinity College Dublin

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W62860524

FWCI:

Cites: 5

Cited by: 5

Related to: 10