Publication Date:
1985-06-14
Description:
The mechanism of irreversible thermoinactivation of an enzyme has been quantitatively elucidated in the pH range relevant to enzymatic catalysis. The processes causing irreversible inactivation of hen egg-white lysozyme at 100 degrees C are deamidation of asparagine residues, hydrolysis of peptide bonds at aspartic acid residues., destruction of disulfide bonds, and formation of incorrect (scrambled) structures; their relative contributions depend of the pH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahern, T J -- Klibanov, A M -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1280-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001942" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Asparagine
;
Chickens
;
Disulfides
;
Hot Temperature
;
Hydrogen-Ion Concentration
;
Kinetics
;
*Muramidase
;
*Protein Denaturation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
