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Regulation of trypsin activity by peptide fraction of an aqueous extract of human placenta used as wound healer.
J Cell Physiol
August 2011
Division of Structural Biology and Bioinformatics, Indian Institute of Chemical Biology (CSIR), Jadavpur, Calcutta, India.
An aqueous extract of human placenta, used as wound healer, shows stabilization of trypsin against autodigestion as one of the peptides of the extract binds very strongly with the protease. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. Inhibition of esterolytic activity and inability to react with p-nitrophenyl-p'-guanidinobenzoate, HCl, an active site directed reagent, by trypsin in presence of a peptide fraction of the extract indicated blocking of the catalytic site of the enzyme.
View Article and Find Full Text PDFIn vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae.
Eur J Biochem
May 1998
College of Pharmacy, Pusan National University, Kumjeong Ku, Korea.
Previously, we purified and characterized a pro-phenol-oxidase (pro-PO) of 79 kDa from coleopteran insect, Holotrichia diomphalia larvae [Kwon et al. (1997) Mol. Cells 7, 90-97].
View Article and Find Full Text PDFComparative study of hemolymph phenoloxidase activity in Aedes aegypti and Anopheles quadrimaculatus and its role in encapsulation of Brugia malayi microfilariae.
Comp Biochem Physiol A Physiol
December 1994
Florida Medical Entomology Laboratory, IFAS, University of Florida, Vero Beach 32962.
Hemolymph phenoloxidase activity of sugar-fed and blood-fed females of Anopheles quadrimaculatus and Aedes aegypti showed similar characteristics. Phenoloxidase was present as an inactive proenzyme in both mosquito species and was partially activated during collection of the hemolymph. In both mosquito species, phenoloxidase activity was modulated by different buffers and activated phenoloxidase did not need Ca2+.
View Article and Find Full Text PDFThe catabolic pathways of streptokinase, plasmin, and activator complex prepared with human plasminogen were studied in mice. (125)I-streptokinase clearance occurred in the liver and was 50% complete in 15 min. Incubation with mouse plasma had no effect on the streptokinase clearance rate.
View Article and Find Full Text PDFp-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin.
Biochem Biophys Res Commun
November 1967
Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.
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