The kinetic studies on the intramolecular SH, S-S exchange reaction of bovine mercaptalbumin.
Bovine mercaptalbumin (BMA) has 17 disulfide bonds and one SH group at Cys-34 which catalyzes the intramolecular SH, S-S exchange reaction (N-A isomerization, molecular aging) in the alkaline region at low ionic strength, resulting in the formation of the aged form (A-form). The aging reaction was completely reversible and strongly affected by environmental factors, such as pH, temperature, ionic strength, Ca2+, nonbranched short-chain fatty acids, etc. Disulfide configuration (or pairing of disulfide bonds) was affected by the environmental factors. Obtained results might support the concept of Klotz (1966) that protein conformation (or three-dimensional structure) is dependent upon (i) the primary structure and (ii) constituents of the solvent.
Kuwata
K
K
Department of Physiology, School of Medicine, Gifu University, Japan.
Era
S
S
Sogami
M
M
D000818:Animals; D002417:Cattle; D004220:Disulfides / Q000378:metabolism*; D005227:Fatty Acids / Q000494:pharmacology; D006358:Hot Temperature; D007536:Isomerism; D009994:Osmolar Concentration; D012709:Serum Albumin / Q000187:drug effects / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000187:drug effects / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism*
D004220:Disulfides; D005227:Fatty Acids; D012709:Serum Albumin; D013438:Sulfhydryl Compounds; C001702:mercaptoalbumin; D012710:Serum Albumin, Bovine