Characterization of arylsulphatase A in a 70 kDa protein isolated from goat spermatozoa having Na+, K+-ATPase inhibitory activity.

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dc.contributor.authorDhara, Tushar K
dc.contributor.authorChatterjee, Madhumouli
dc.contributor.authorBera, Rabindranath
dc.contributor.authorSen, Parimal C
dc.date.accessioned2011-11-09T08:09:22Z
dc.date.available2011-11-09T08:09:22Z
dc.date.issued2009-06
dc.description.abstractA protein having inhibitory effect on Na+, K+-ATPase as well as showing arylsulphatase A activity (ASA) was isolated from the cytosolic fraction of goat spermatozoa and characterized biochemically. The molecular mass of the protein was found to be 70 kDa (P70) on 10% SDS-PAGE after 35% ammonium sulphate precipitation, followed by hydroxyapatite column chromatographic separation. The isoelectric point (pI) of the protein was found to be 4.9. The sequencing results of first ten N-terminal amino acid residues of protein showed 100%, 90%, and 80% homology with N-terminal 18-27 amino acid residues of mice, pig and human testicular ASA, respectively. The optimum pH, temperature and incubation time for maximum ASA activity of the protein was 5.5, 37°C and 30 min respectively. The ASA activity of protein and AS from a commercial source was studied with respect to the sensitivity to different metal ions, vanadate, carbonyl compounds and ascorbate. Inhibition of AS activity of P70 by silver nitrate suggested that it was related to ASA. Comparable effects of different polyunsaturated fatty acids (eicosapentaenoic and docosahexaenoic acids) and purified anti P70-antibody on P70 and AS from commercial source were observed. The findings suggested that protein was novel in nature, having both regulatory and catalytic functions and showed similarities with the ASA reported from different sources.en_US
dc.identifier.citationDhara Tushar K, Chatterjee Madhumouli, Bera Rabindranath, Sen Parimal C. Characterization of arylsulphatase A in a 70 kDa protein isolated from goat spermatozoa having Na+, K+-ATPase inhibitory activity. Indian Journal of Biochemistry & Biophysics. 2009 June; 46(3): 230-236.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/135198
dc.language.isoenen_US
dc.source.urihttps://nopr.niscair.res.in/bitstream/123456789/4584/1/IJBB%2046%283%29%20230-236.pdfen_US
dc.subjectArylsulphatase Aen_US
dc.subjectGoat spermatozoaen_US
dc.subjectInhibitor of Na+en_US
dc.subjectK+-ATPaseen_US
dc.subject70 kDa Proteinen_US
dc.subject.meshAcrosome Reaction
dc.subject.meshAnimals
dc.subject.meshCerebroside-Sulfatase --chemistry
dc.subject.meshCerebroside-Sulfatase --genetics
dc.subject.meshCerebroside-Sulfatase --metabolism
dc.subject.meshEnzyme Inhibitors --metabolism
dc.subject.meshEpididymis --cytology
dc.subject.meshGoats
dc.subject.meshMembrane Proteins --chemistry
dc.subject.meshMembrane Proteins --genetics
dc.subject.meshMembrane Proteins --metabolism
dc.subject.meshMolecular Weight
dc.subject.meshSodium-Potassium-Exchanging ATPase --antagonists & inhibitors
dc.subject.meshSodium-Potassium-Exchanging ATPase --chemistry
dc.subject.meshSodium-Potassium-Exchanging ATPase --genetics
dc.subject.meshSodium-Potassium-Exchanging ATPase --metabolism
dc.subject.meshSperm Capacitation
dc.subject.meshSpermatozoa --chemistry
dc.subject.meshSpermatozoa --cytology
dc.subject.meshSpermatozoa --metabolism
dc.titleCharacterization of arylsulphatase A in a 70 kDa protein isolated from goat spermatozoa having Na+, K+-ATPase inhibitory activity.en_US
dc.typeArticleen_US
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