ISSN:
1573-4943
Schlagwort(e):
Ribulose 1,5 bisphosphate carboxylase/oxygenase
;
enzyme protection
;
enzyme inactiviation
;
protein oxidation
;
protein structural stability (Citrus)
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
Notizen:
Abstract When assayedin vitro, the activity of the photosynthetic enzyme ribulose 1,5 bisphosphate carboxylase/oxygenase is both enhanced and protected from spontaneous decay by exogenous proteins such as hemoglobin, serum albumin, and aldolase. Other proteins and amino acids tested are either ineffective (lysozyme, ferritin, lysine, and cysteine) or afford only partial protection (catalase, glycine, and phenylalanine). Protective proteins do not bind to, or exchange disulfides with, ribulose 1,5 bisphosphate carboxylase/oxygenase. Since their effect can be mimicked by reductively treated detergents such as Triton X-100, it appears that proteins protect from decay by quenching the spontaneous oxidative degradation and inhibiting surface adsorption which could lead to enzyme unfolding. Release of adsorbed molecules from the container surface is likely to be the cause of carboxylase activity enhancement.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF01025627
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