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V Deshpande

Publications and source records attributed to V Deshpande.

12 recordsLinked to original sources
PubMed1991

Immunoaffinity purification of glucose/xylose isomerase from Streptomyces.

A procedure was developed to purify glucose/xylose isomerase from cell extract of Streptomyces sp. NCIM 2730 using immunoaffinity chromatography. High-titer polyclonal antibodies were raised in rabbit using electrophoretically homogeneous glucose/xylose isomerase as an antigen. The specificity of antibodies was confirmed by double immunodiffusion, rocket electrophoresis, and Western-blot ELISA, which revealed the presence of a single immunoreactive protein with an Mr of 40,000. The antibodies recognized 2-3 antigenic determinants/mol of enzyme and were found to partially neutralize the enzymatic activity in an immunotitration experiment. The affinity gel was prepared by coupling antibodies at pH 10.0 to divinyl sulfone-activated Sepharose CL-4B. The glucose/xylose isomerase purified by immunoaffinity chromatography yielded 75% recovery with a single enzymatically active protein band on gel electrophoresis and showed specific activity of 16 U/mg. The crossreaction of the antibodies with glucose isomerase from other actinomycetes indicated that they share common epitopes.

Aldose-Ketose Isomerases↗
PubMed1991

Buffalo thyroglobulin.

1. Buffalo thyroglobulin is the major iodoprotein of buffalo thyroid with a sedimentation coefficient of 19 S and an apparent molecular mass of 685 kDa. 2. The protein is rich in iodine (1-2%) and thyroxine bound iodine (75%), unlike thyroglobulins of other mammalian species. 3. As a glycoprotein, it has the same sugar residues as noted for other thyroglobulins, and the total carbohydrate content varies from 8.41 to 9.61%. 4. Amino acid composition of buffalo thyroglobulin is similar to other species. However, the protein has 2% more proline than other mammalian thyroglobulins. 5. Glutamic acid is the sole N-terminal amino acid of buffalo thyroglobulin, in contrast to aspartic acid or asparagine for several other species. 6. The quaternary structure of the protein appears to be comprised of eight non-identical subunits.

Amino Acids↗
PubMed1990

Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.

N-Bromosuccinimide (NBS) completely inactivated xylanases from Chainia and alkalophilic and thermophilic (AT) Bacillus with a concomittant decrease in absorption at 280 nm and with second-order rate constants of 10,500 and 5000 M-1.min-1, respectively at pH 6.0 and 25 degrees C. The kinetic analysis of inactivation indicated that one and three tryptophan residues were essential for the xylanase activity from Chainia and Bacillus, respectively. The xylanases were also inhibited by 2-hydroxy-5-nitrobenzyl bromide (HNBB). The modification of cysteine residues by p-hydroxymercurybenzoate (PHMB) and N-ethylmaleimide did not cause a loss in activity of the xylanase from Bacillus, whereas that from Chainia was completely inactivated. The kinetics of inactivation revealed the involvement of one cysteine residue for xylanase from Chainia with a second-order rate constant of 50,000 M-1.min-1. The PHMB-modified enzyme failed to show the presence of titrable -SH groups. Xylan afforded complete protection against inactivation by NBS, HNBB and PHMB, indicating the involvement of tryptophan and cysteine residues at the substrate-binding region of the enzyme.

Bacillus↗
PubMed1990

N-terminal groups of buffalo thyroglobulin.

N-Terminal analysis of purified buffalo thyroglobulin by the fluorodinitrobenzene method of Sanger yielded about 1.5 moles of DNP-glutamic acid per mole of buffalo thyroglobulin. No water-soluble DNP-amino acid was detectable as N-terminal. The presence of glutamic acid has been confirmed by Edman degradation and characterization of the PTH-amino acid in different solvent systems, and also after regeneration of free amino acid from PTH-amino acid in butanol-acetic acid-water (4:1:5, v/v) system. This is in contrast to the occurrence of aspartic acid or asparagine as N-terminals for several other mammalian thyroglobulins.

Amino Acids↗
PubMed1988

Induction and catabolite repression of cellulase in Penicillium funiculosum.

The regulation of endoglucanase synthesis in Penicillium funiculosum is investigated using a method based on the viscosity lowering effect on carboxy methyl cellulose (CMC) by endoglucanase. Cellobiose (1 mg/L) causes induction, whereas glucose (5 g/L) does not repress the enzyme formation. Lactose (5 g/L) has no effect on the synthesis of cellulase. Avicel and cellulose powder (CP) are the best inducers of cellulase and xylanase activity. Both endoglucanase and xylanase activity were induced by CMC, whereas xylan induced only xylanase activity. The effect of protease on induction of cellulase activity is discussed.

Caseins↗
PubMed1979

Unusual leiomyoblastoma of the stomach.

Only about 250 cases of benign gastric leiomyoblastoma of the stomach have been reported. Most occur in the smooth muscle of the antrum, and may be intramural, intraluminal, or exogastric in position. A pedunculated gastric leiomyoblastoma occurs less frequently, and those containing radiographically identifiable calcifications are extremely rare.

Aged↗