Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Sarvagya S. Katiyar"'
Publikováno v:
Journal of Food Biochemistry. 30:12-20
The extracellular dextransucrase (sucrose: 1,6-α-D-glucan 6-α-D-glucosyltransferase EC 2.4.1.5) from Leuconostoc mesenteroides NRRL B-512F was purified by phase partitioning using poly(ethylene) glycol (PEG) and dextran generated by dextransucrase.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1be71be5a3ca5b1e97e0b131055f68cb
https://doi.org/10.1111/j.1745-4514.2005.00047.x
https://doi.org/10.1111/j.1745-4514.2005.00047.x
Publikováno v:
European Journal of Biochemistry. 130:177-184
Pigeon liver fatty acid synthetase was inactivated by treatment with S-(4-bromo-2,3-dioxobutyl)-CoA. This inactivation is fast, irreversible and dependent on both time and inhibitor concentration. It is also specific and selective as only the 3-oxoac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23cfa39d48f608333755d2054bb19027
https://doi.org/10.1111/j.1432-1033.1983.tb07134.x
https://doi.org/10.1111/j.1432-1033.1983.tb07134.x
Autor:
Sarvagya S. Katiyar, Arun Goyal
Publikováno v:
Journal of Enzyme Inhibition. 13:147-160
The kinetics of inactivation of Leuconostoc mesenteroides NRRL B-512F dextransucrase by o-phthalaldehyde showed that the reaction followed pseudo-first order reaction. The loss of enzyme activity was concomitant with an increase in fluorescence at 41
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f6628621b0a91be18eb941db1f5539c
https://doi.org/10.3109/14756369809035833
https://doi.org/10.3109/14756369809035833
Autor:
Sarvagya S. Katiyar, Anjali Pandey
Publikováno v:
Journal of Enzyme Inhibition. 11:141-149
Yeast glutathione reductase was inactivated by the bifunctional reagent, o-phthalaldehyde. The initial rate of inactivation followed pseudo-first order kinetics. Fluorescence spectral properties of modified enzyme indicated the formation of an isoind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9eddb9e7a0807b447955ec1721f8fc77
https://doi.org/10.3109/14756369609036541
https://doi.org/10.3109/14756369609036541
Autor:
Sarvagya S. Katiyar, Arun Goyal
Publikováno v:
The Journal of General and Applied Microbiology. 42:81-85
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f668c3c796a74f2cfd61739b99c5572
https://doi.org/10.2323/jgam.42.81
https://doi.org/10.2323/jgam.42.81
Publikováno v:
Polymer International. 37:287-290
The radical polymerization of acrylonitrile (AN) with α-picolinium p-chlorophenacylid (α-PCPY) as initiator using carbon tetrachloride as inert solvent was investigated at 50°C. The polymerization follows ideal kinetics: the exponent values calcul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0928bb223837f3ee3479f78e862b9b22
https://doi.org/10.1002/pi.1995.210370407
https://doi.org/10.1002/pi.1995.210370407
Autor:
Arun Goyal, Sarvagya S. Katiyar
Publikováno v:
Journal of Microbiological Methods. 20:225-231
Leuconostoc mesenteroides NRRL B-512F dextran sucrase (sucrose: 1,6-α- d -glucan 6-α- d -glucosyltransferase EC 2.4.1.5) (1.4 U/ml culture supernatant, specific activity 0.58 U/mg protein) was subjected to fractionation by polyethylene glycol (PEG)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07b12915db112ec1942292f0eeb46107
https://doi.org/10.1016/0167-7012(94)90007-8
https://doi.org/10.1016/0167-7012(94)90007-8
Autor:
Sarvagya S. Katiyar, Saifuddin Sheikh
Publikováno v:
Journal of Enzyme Inhibition. 8:39-50
The effect of o-phthalaldehyde on octopine dehydrogenase inactivation has been studied. o-Phthalaldehyde binds to the proximal cysteine and lysine residues of the enzyme leading to the formation of isoindole derivative. Double inhibition studies with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d65813ebdcc3ff3674254f4d25236be0
https://doi.org/10.3109/14756369409040775
https://doi.org/10.3109/14756369409040775
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1203:276-281
Inactivation of rabbit muscle creatine kinase by o-phthalaldehyde was investigated. The loss of enzyme activity was concomitant with the increase in fluorescence intensity at 410 nm. The modified enzyme showed a characteristic absorption peak at 336
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d25a0c0084501d7193f87c1bbf23f8bc
https://doi.org/10.1016/0167-4838(93)90094-8
https://doi.org/10.1016/0167-4838(93)90094-8
Autor:
Sarvagya S. Katiyar, Saifuddin Sheikh
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1202:251-257
Thiol-specific reagents, p-chloromercuricphenyl sulfonic acid (PCMS), 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and N-ethyl-maleimide (NEM), incubated with octopine dehydrogenase resulted in the loss of catalytic activity. The kinetic profile of PC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fadff52e366c8cb45549c29226cae2d
https://doi.org/10.1016/0167-4838(93)90012-g
https://doi.org/10.1016/0167-4838(93)90012-g