| Literature DB >> 2504146 |
T K Datta1, P S Basu, P K Datta, A Banerjee.
Abstract
A monomeric glycoprotein (SGP) of Mr 32,000 was isolated to purity from scorpion (Heterometrus bengalensis) haemolymph by (NH4)2SO4 fractionation, chromatofocusing and h.p.l.c. The homogeneity of SGP is confirmed by polyacrylamide-gel electrophoresis. SGP is soluble in 100%-satd. (NH4)2SO4 solution. Needle-shaped crystals of SGP were obtained in an aqueous environment. The glycan part of the molecule contains arabinose, which does not commonly occur in animal glycoproteins. Amino acid analysis demonstrated a preponderance of glycine, tyrosine and glutamic acid. SGP enhances phenol oxidase (EC 1.14.18.1) activity.Entities:
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Year: 1989 PMID: 2504146 PMCID: PMC1138699 DOI: 10.1042/bj2600525
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857