Studies on some aspects of peroxidase from submaxillary gland |
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Authors: | Manjusree Bal Ganes Sen Usha Mahajani Asoke G. Datta |
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Affiliation: | Department of Physiology, Indian Institute of Experimental Medicine, 4, Raja S. C. Mullick Road, Calcutta-32, India |
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Abstract: | A peroxidase has been purified 25- to 30-fold over crude homogenate from goat submaxillary gland, which shows a single band of protein on polyacrylamide gel electrophoresis at four different pH values (4.6–10.0). A molecular weight (Mr) of approximately 2 × 104 per heme binding site has been found. The molecular weight of the enzyme determined by Sephadex-gel filtration method, appeared to be 4 × 104. The sedimentation pattern of the purified enzyme shows a symmetrical peak, although there was evidence of some small heterogenous material near the meniscus. The sedimentation coefficient of the enzyme (so 20wat 0.4% of the enzyme concentration) was found to be 4.18, which indicates the molecular weight of the enzyme to be approximately 6 × 104. |
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