Zobrazeno 1 - 10 of 12 pro vyhledávání: '"B C, Shenoy"'
1
Effect of deletion from the carboxyl terminus of the 12 S subunit on activity of transcarboxylase
Autor: S B, Woo, B C, Shenoy, H G, Wood, W J, Magner, G K, Kumar, H, Beegen, D, Samols
Publikováno v: The Journal of biological chemistry. 268(22)
Transcarboxylase from Propionibacterium shermanii is a biotin-containing enzyme which catalyzes the reversible transfer of a carboxyl group from methylmalonyl-CoA to pyruvate. The central hexameric 12 S subunit of the enzyme associates with six 6 S s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3becc09e65557ea41a2fa29d1ce50ac
https://pubmed.ncbi.nlm.nih.gov/8344927
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2
Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
Autor: B C, Shenoy, G K, Kumar, D, Samols
Publikováno v: The Journal of biological chemistry. 268(3)
Transcarboxylase, a multisubunit enzyme containing 12 S, 5 S, and 1.3 S subunits, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate (overall reaction) via two partial reactions. In the first partial reaction, a carboxyl gr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1282be290bc41e3250f0a9a22a8b3082
https://pubmed.ncbi.nlm.nih.gov/8420991
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3
The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
Autor: B C, Shenoy, Y, Xie, V L, Park, G K, Kumar, H, Beegen, H G, Wood, D, Samols
Publikováno v: The Journal of biological chemistry. 267(26)
Almost all biotin enzymes contain the conserved tetrapeptide Ala-Met-Bct-Met (Bct, N epsilon-biotinyl-L-lysine). In the 1.3 S biotinyl subunit of transcarboxylase (TC), this sequence is present between positions 87 and 90. The conserved nature of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b559c40f00b9326c390e81ee635d6422
https://pubmed.ncbi.nlm.nih.gov/1526981
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5
Purification and properties of diaminopimelate decarboxylase ofMicrococcus glutamicus
Autor: Meena Lakshman, B. C. Shenoy, M. R. Raghavendra Rao
Publikováno v: Journal of Biosciences. 3:89-103
Diaminopimelate decarboxylase (EC 4.1.1.20) ofMicrococcus glutamicus ATCC 13059 was purified to homogeneity. The enzyme had an apparent molecular weight of 191,000 as determined by gel filtration on Sephadex G-200. At protein concentrations of 20 and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::407bf359b1bcc45a87b5685340abf9e2
https://doi.org/10.1007/bf02702651
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6
Studies on plant gums. Role of calcium in polysaccharide-protein interaction in the neem (Azadirachta indica) gum
Autor: T. N. Pattabiraman, B. Ramakrishna Nayak, B. C. Shenoy
Publikováno v: Journal of Biosciences. 1:61-68
The partial removal of tightly bound Ca2+ from dialysed neem (Azadirachta indica) gum, resulted in the release of a basic protein from a highly anionic polysaccharide-protein complex as evidenced by chromatographic studies on TEAE-cellulose. Complete
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::118a5f0fc7222959d1b5190c77509d1c
https://doi.org/10.1007/bf02702887
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7
Fungal glucoamylases
Autor: B. C. Shenoy, M. R. Raghavendra Rao, A. G. Appu Rao, L. C. Katwa
Publikováno v: Journal of Biosciences. 7:399-419
The purification and properties of glucoamylase (α-l,4-glucan glucohydrolase, EC 3.2.1.3) from different fungal sources have been compared. The studies on the conformation and activity of the native enzyme at a function of pH, temperature, substrate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::41415a0d178a4ab72c2ac9434fdfd9d0
https://doi.org/10.1007/bf02716801
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8
Structure and stability of glucoamylase II fromAspergillus niger: A circular dichroism study
Autor: A. G. Appu Rao, B. C. Shenoy, M. R. Raghavendra Rao
Publikováno v: Journal of Biosciences. 6:601-611
Glucoamylase II (EC 3.2.1.3) fromAspergillus niger has 31 % α-helix, 36 %Β- structure and rest aperiodic structure at pH 4.8 as analysed by the method of Provencher and Glockner (1981,Biochemistry, 20,33). In the near ultra-violet circular dichrois
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a1993e1c4b1d87b990a05ede9eaf8056
https://doi.org/10.1007/bf02702702
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9
Aspartokinase of a lysine producing mutant ofMicrococcus glutamicus
Autor: B. C. Shenoy, Meena Lakshman, M. R. Raghavendra Rao
Publikováno v: Journal of Biosciences. 3:57-67
Aspartokinase fromMicrococcus glutamicus AEC RN-13-6/1 [a homoserine requiring, S-(2-aminoethyl)-L-cysteine resistant, lysine producing strain] was purified 71 fold. The partially purified enzyme was inhibited by L-lysine. L-threonine, L-methionine,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bbac471546ae5b028b2bfa4740c0ad97
https://doi.org/10.1007/bf02703348
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10
Effect of chemical modification on struture and activity of glucoamylase fromAspergillus candidus andRhizopus species
Autor: B. C. Shenoy, A. G. Appu Rao, M. R. Raghavendra Rao
Publikováno v: Journal of Biosciences. 11:339-350
The histidine, tyrosine, tryPtoPhan and carboxyl grouPs in the enzyme glucoamylase fromAsPergillus Candidus andRhizoPus sPecies were modified using grouP sPecific reagents. Treatment of the enzyme with diethylPyrocarbonate resulted in the modificatio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::71f73ef0959e0ee2d4a4381434bbb3bb
https://doi.org/10.1007/bf02704684
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