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11.
R K Sharma 《Biochemical and biophysical research communications》1991,181(1):493-497
Polyclonal antibodies raised against bovine heart high molecular weight calmodulin-binding protein were used to study the distribution of this protein in diverse bovine tissues. The high molecular weight calmodulin-binding protein, in addition to bovine heart, is also present in lung and brain at much lower levels, but not in skeletal muscle, spleen, kidney or uterus. 相似文献
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K Muralidhar T Rajendrakumar H P Sharma 《Indian journal of biochemistry & biophysics》1992,29(2):168-172
Lutropin (LH-1) from water buffaloes has been shown to exhibit microheterogeneity in the N-terminal amino-acid sequence of its alpha-subunit. The beta-subunit did not exhibit such microheterogeneity. Another protocol of purification yielded a preparation of buffalo LH (bu LH-2) different from the buffalo LH-1 in certain physico-chemical properties like ease of dissociation into subunits, sugar composition, isoelectric point, and elution profile on S-200. Data appear to indicate the presence of more than one form of buffalo lutropin. 相似文献
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Summary On a Typic Ustochrept soil incorporation of 10 tons/ha of a green manure plus submergence for 10 days followed by raising upland nursery checked iron chlorosis. In contrast, presubmergence with and without FYM and iron sulfate or pyrite were a failure. Nor weekly sprays with 3.0% iron sulfate were found very effective. The success of green manure plus submergence was associated with the mobilization of soil iron as a result of intense reduction and its subsequent retention in available form at a sufficient high level during the growth of upland nursery. 相似文献
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Ten species of Lepadella Bory de St. Vincent, 1826, including one new species and one new form, are documented from North-Eastern India. Two of these species are new records from this country and six are new reports from N.E. region. Comments are also made on the status and distribution of various Indian taxa. 相似文献
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R K Gaur S Paliwal P Sharma K C Gupta 《Journal of biochemical and biophysical methods》1989,18(4):323-329
A simple and sensitive method for the quantitative determination of free amino groups on solid support is described. This approach is a modification of Ngo's [(1986) J. Biochem. Biophys. Methods 12, 349-354] method reported earlier. The method is based on the reaction of the solid support with an excess of 5'-O-(4,4'-dimethoxytrityl)-thymidine-3'-O-(2,4-dinitrophenyl) succinate (DTDS) in the presence of a catalytic amount of 4-dimethylaminopyridine. After removing the excess reagent, solid support is treated with perchloric acid to release 4,4'-dimethoxytrityl cation into the solution. The released 4,4'-dimethoxytrityl cation, which has a strong absorption at 498 nm (epsilon 498 = 70,000), is then determined spectrophotometrically. A comparative study of DTDS, N-succinimidyl-3-(2-pyridyldithio)propionate and 4,4-dimethoxytrityl chloride is also included. The method was found to be very useful to determine those amino groups which are available for functionalization of solid supports, especially, monitoring the functionalization of solid supports for affinity chromatography and synthesis of biopolymers. 相似文献