Chemical modification and complex formation studies with jack bean proteinase inhibitor.

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dc.contributor.authorKumari, N Nen_US
dc.contributor.authorPattabiraman, T Nen_US
dc.date.accessioned1991-10-01en_US
dc.date.accessioned2009-05-27T09:23:32Z
dc.date.available1991-10-01en_US
dc.date.available2009-05-27T09:23:32Z
dc.date.issued1991-10-01en_US
dc.description.abstractPretreatment of the purified jack bean inhibitor with enterokinase activated human pancreatic preparation for 1 hr decreased its inhibitory capacity against crystalline bovine alpha-chymotrypsin by 30% but did not affect its trypsin inhibitory activity. Preincubation of the inhibitor with bovine chymotrypsin for 60 min resulted in partial loss of the inhibitory potency. Complex formation studies by gel chromatography on Sephadex G-100 indicated that the trypsin-inhibitor and chymotrypsin-inhibitor complexes dissociated to release inactivated inhibitor and active proteinases. Gel chromatography of the inhibitor in presence of 1.5 M ammonium sulphate indicated that the inhibitor showed a tendency to aggregate without loss of biological activity. However, in 4.2 M salt medium after 3 hr, antichymotryptic activity was lost completely without any effect on antitryptic activity. Treatment with methylamine, a nucleophile, caused a greater loss of antichymotryptic activity. Trinitrobenzene sulphonate and ethylacetamidate, the amino group modifiers, affected only the antichymotryptic activity. Treatment with ninhydrin, a specific arginine modifier, at pH 9.0 abolished the antitryptic activity whereas only 50% of the antichymotryptic activity was lost. Diethylpyrocarbonate, a histidine reagent, also decreased only the antitryptic activity. Modification of tryptophan and cysteine residues of the inhibitor had no effect on its inhibitory potency. Treatment with mercaptoethanol and sodium borohydride caused nearly 50% loss of antitryptic and antichymotryptic activities. Chloramine-T, a reagent that modifies methionine residues, inactivated the inhibitor.en_US
dc.description.affiliationDepartment of Physiology, Kasturba Medical College, Manipal, Karnataka, India.en_US
dc.identifier.citationKumari NN, Pattabiraman TN. Chemical modification and complex formation studies with jack bean proteinase inhibitor. Indian Journal of Biochemistry & Biophysics. 1991 Oct-Dec; 28(5-6): 425-33en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27364
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshFabaceae --chemistryen_US
dc.subject.meshPlants, Medicinalen_US
dc.subject.meshProtease Inhibitors --chemistryen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.titleChemical modification and complex formation studies with jack bean proteinase inhibitor.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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