Year: 1990
Type: article
Abstract: White-gourd protease was rapidly inactivated by methylene blue catalysed photooxidation at pH 8.0 and 200.The rate of inactivation was pH-dependent and became slower at lower pH values, suggesting the involvement of some histidine residues in the inactivation.Changes in the amino acid composition occurred only with histidine residues.One mole or more of histidine residues in the molecule are essential importance in the catalytic function of white-gourd protease.
Authors: KANEDA, Makoto, 金田, 信, MIYASHITA, Hideto, 宮下, 秀人, UCHIKOBA, Tetsuya, 内木場, 哲也
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W7022514736