Year: 1989
Type: article
Abstract: The hydrolysis of 3 distinct substrates by cathepsin E from human red blood cells and gastric mucosa was measured in the presence and absence of physiologically relevant concentrations of ATP. At pH values below about 5.0, the nucleotide was without effect. However, at pH 5.8, whereas cathepsin E was virtually inactive by itself, it was restored to full activity (kcat) by ATP and the non-hydrolysable methylene-ATP analogue. At still higher pH values, kcat progressively diminished but significant levels of cathepsin E activity were readily detectable at pH 7.0. The specificity of this stabilisation effect was examined.
Source: FEBS Letters
Authors: D.J. Thomas, A.D. Richards, R.A. Jupp, E. Ueno, K. Yamamoto, I.M. Samloff, B.M. Dunn, J. Kay
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1971490170