Co2+ - mediated time - and temperature - dependent activation of neutral α-D-mannosidase from monkey brain

Mathur, R. ; Panneerselvam, K. ; Balasubramanian, A. S. (1988) Co2+ - mediated time - and temperature - dependent activation of neutral α-D-mannosidase from monkey brain Biochemical Journal, 253 (3). pp. 677-685. ISSN 0264-6021

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Official URL: http://www.biochemj.org/bj/253/bj2530677.htm

Abstract

Neutral alpha-D-mannosidase from monkey brain was purified by Co2+-chelate affinity chromatography and immunoadsorbent affinity chromatography. The purified enzyme, with subunit Mr 45,000, was essentially homogeneous with only traces of two contaminant proteins as revealed by SDS/polyacrylamide-gel electrophoresis and AgNO3 staining. The purified enzyme, on preincubation with Co2+ at 37 degrees C or 60 degrees C followed by assay, showed a time-dependent enhancement in activity. The enhanced activity of the enzyme persisted even after removal of the Co2+. Bacitracin could partially prevent the activation. An aminopeptidase activity that was stimulated by Co2+ both at 37 degrees C and at 60 degrees C was present in the purified enzyme. After preincubation of the enzyme with Co2+ there was evidence for the release of amino acids, as revealed by t.l.c., but the Mr determined by SDS/polyacrylamide-gel electrophoresis was not appreciably altered. It is suggested that a Co2+-stimulated thermostable aminopeptidase, inseparable from the neutral mannosidase, may be involved in the stimulation of neutral mannosidase activity during its preincubation with Co2+.

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