Renaturation of reduced hen egg white lysozyme containing two blocked sulfhydryl groups

Journal Article · Wed Oct 01 00:00:00 EDT 1980 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(80)84967-8· OSTI ID:6760755

Acharya, A S; Taniuchi, H

Formation of native lysozyme from the reduced form involves many pathways in two processes: incorrect pairing of half-cystine residues by oxidation and rearrangement of disulfide (SS) bonds. The energy barrier against suflhydryl (SH)-disulfide interchange of the native or nativelike species thus formed causes accumulation of these species. For example, the enzymatically active isomers containing three presumably native SS bonds and one open SS bond may be thermodynamically favorable over the nonnative isomers and can be formed from reduced lysozyme or lysozyme containing scrambled SS bonds by nonobligatory and flexible pathways. As an extension of these observations formation of nativelike species from reduced lysozyme containing the average of two carboxymethyl (CM)-cysteine was investigated.

• Research Organization: National Institutes of Health (NIH), Bethesda, MD (United States)
• OSTI ID: 6760755
• Journal Information: Biophys. J.; (United States), Vol. 32:1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
LYSOZYME
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL PATHWAYS
CARBON 14 COMPOUNDS
CHICKENS
EGGS
ENERGY TRANSFER
PROTEIN DENATURATION
THERMODYNAMICS
ANIMALS
BIRDS
ENZYMES
FOWL
GLYCOSYL HYDROLASES
HYDROLASES
KINETICS
LABELLED COMPOUNDS
O-GLYCOSYL HYDROLASES
REACTION KINETICS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques