Purification of a unique glycoprotein that enhances phenol oxidase activity in scorpion (Heterometrus bengalensis) haemolymph.
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.
Datta
T K
TK
Indian Institute of Chemical Biology, Calcutta.
Basu
P S
PS
Datta
P K
PK
Banerjee
A
A
D000818:Animals; D004156:Catechol Oxidase / Q000097:blood*; D006023:Glycoproteins / Q000302:isolation & purification* / Q000502:physiology; D006458:Hemolymph / Q000201:enzymology / Q000378:metabolism*; D014442:Monophenol Monooxygenase / Q000097:blood*; D012605:Scorpions / Q000201:enzymology / Q000378:metabolism*
D006023:Glycoproteins; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase