Biomedical subjects
Publications and source records attributed to R Kalyani.
Colonic carcinoma in young adults are rare and has a higher mortality and morbidity because of poor histological type and delay in diagnosis. We are reporting two cases of mucinous adenocarcinoma of caecum and sigmoid colon in young males.
Primary adenocarcinoma of fallopian tube is the rarest gynecological malignancy of female genital system which is usually misdiagnosed as ovarian tumour or tubo-ovarian mass. We present a case in a 40 year old female.
Reporting three rare cases of multiple primary cancers. Case one and two were a synchronous presentation of primary gastric carcinoma and renal carcinoma, gastric carcinoma and papillary carcinoma thyroid. Case 3 was metachronous presentation of squamous cell carcinoma of the oral cavity and hepatocellular carcinoma.
The mRNA encoding an agouti related protein (ART) of unknown biochemical function was previously reported to be up-regulated in the hypothalamus of two genetically obese mouse strains. We have expressed human ART as a secreted protein in COS-7 cells, and show that recombinant ART is functionally active in inhibiting the binding of a radiolabeled alpha-melanocyte stimulating hormone (alpha-MSH) analog to the human melanocortin-3 (MC-3) and melanocortin-4 (MC-4) receptors, while it is not a potent inhibitor of the human melanocortin-5 (MC-5) receptor. ART is an antagonist of the human MC-3 and MC-4 receptors as determined in functional assay. ART appears to be approximately 100-fold more potent than agouti with reference to the MC-3R and MC-4R binding affinity. These data suggest that ART may be a physiological regulator of feeding behavior.
beta-D-galactosidase (beta-D-galactoside galactohydrolase, E.C. 3.2.1.23) activity was localised in the digestive tract of Setaria digitata. The enzyme extract shows maximum activity in the pH range between 3.5 and 5.0 and at 45 degrees C. The enzyme shows the Km value of 3.636 mM for the substrate 6-bromo-2-naphthyl beta-D-galactoside and Vmax of 28.57 nmol 6-bromo-2-naphthol liberated mg-1 protein min-1. Activation/inhibition of the enzyme by various ions, medicinal plants and drugs has been studied. Polyacrylamide gel electrophoresis revealed that the enzyme exists as single form. The medicinal plants and the drug filarin effectively inhibit the enzyme. The significance of these results are discussed in relation to chemotherapy.
This technique for localizing catecholic residues in biological samples is based on the condensation of Besthorn's hydrazone (3-methyl-2-benzothiazolinone hydrazone hydrochloride (MBTH) with quinone residues obtained by the oxidation of catechols in the presence of ammonia. The product is a dark pink MBTH-quinone compound. This method is very sensitive and positive to catechol even at the 0.05 microgram level and the final product is chemically stable.
The precursors of sclerotin such as phenol and phenoloxidase have been localized in the mantle tissue of Achatina fulica based on incubation study. The phenolic compound exists as dopyl protein. The mantle shows both mono- and diphenoloxidase activity as evidenced by the effective oxidation of tyrosine and Dopa. The enzyme shows a pH optimum of 6.5. Chemicals acting on the mantle phenoloxidase reveal that it contains sulphydryl groups. Studies on the effect of temperature show that the heat inactivation of the enzyme is reversed at higher temperatures. Electrophoretic study indicates that the enzyme exists in multiple forms. Results are discussed in relation to sclerotization.
A 7% sodium dodecyl sulfate (SDS) polyacrylamide slab gel electrophoresis was carried out to study the molecular weight of blood and cuticular phenoloxidase from different crustaceans. In Uca lacteus de Haan, Scylla serrata Forskal and Ocypode platytarsis Milne Edwards, the apparent molecular weight of cuticular phenoloxidase is higher than that of blood phenoloxidase, whereas the molecular weights of cuticular phenoloxidase isozymes of Emerita emeritus L. are lower than those of blood phenoloxidase isozymes. In Metapenaeus monoceros Fabricius, the blood phenoloxidase shows a molecular weight of 250,000 and the cuticular phenoloxidase shows two isozymes with molecular weights of 350,000 and 250,000. The individuality of blood phenoloxidase and cuticular phenoloxidase and their roles are discussed.
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