Hysteretic enzyme adaptation to environmental pH: Change in storage pH of alkaline phosphatase leads to a pH-optimum in the opposite direction to the applied change

Biophysical Chemistry

Volumn 77, Issue 2-3, 1999, Pages 99-109

  Behzadi, Amrollah ^a   Hatleskog, Rune ^a   Ruoff, Peter ^a  

^a UNIVERSITY OF STAVANGER   (Norway)

Author keywords

Alkaline phosphatase; Diprotic model; Hysteretic enzymes; Kinetics; pH; Protein fluorescence

Indexed keywords

ALKALINE PHOSPHATASE; ENZYME;

ARTICLE; CATTLE; FLUORESCENCE; MODEL; NONHUMAN; PH; PRIORITY JOURNAL; STORAGE; ULTRAFILTRATION;

ALKALINE PHOSPHATASE; ANIMALS; CATTLE; HYDROGEN-ION CONCENTRATION; INTESTINES; KINETICS; PHENYLALANINE; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; TYROSINE;

EID: 0033007814     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(99)00013-7     Document Type: Article

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