نتایج جستجو برای: binding lectin deficiency

تعداد نتایج: 555860  

Journal: :Cancer research 1980
R J Stockert F F Becker

The lectin hepatic binding protein has a specific binding capacity for desialylated serum glycoproteins and is limited to hepatocyte membranes. This binding capacity was reduced by approximately 60% in the neoplastic nodules which resulted from exposure of rat livers to N-2-acetylaminofluorene. The binding capacity of the primary hepatocellular carcinomas which resulted from this regimen was re...

2011
Subramaniya Bharathi Raja Malliga Raman Murali Nirmal Kasinathan Kumar Sivasitambaram Niranjali Devaraj

Lectins are a class of ubiquitous proteins/glycoproteins that are abundantly found in nature. Lectins have unique carbohydrate binding property and hence have been exploited as drugs against various infectious diseases. We have isolated one such novel lectin from the fruit pulp of Aegle marmelos. The isolated lectin was partially characterised and its effect against Shigella dysenteriae infecti...

Journal: :The Biochemical journal 1979
B Bernard M Aubery R Bourrillon

The toxic effect of Ricinus lectin RCA I, as estimated by the inhibition of [3H]leucine incorporation, was investigated on chick-embryo fibroblasts at different stages of development. There appeared to be a differential susceptibility of chick-embryo fibroblasts to lectin RCA I. Fibroblasts from 16-day embryos were the most sensitive to its toxic effect in terms of both concentration and time, ...

Journal: :Cancer research 1988
E Paietta R Gallagher P H Wiernik R J Stockert

A novel mammalian lectin activity responsive to monocytic differentiation is described in the human promyelocytic leukemia cell line HL-60. Glycoprotein binding indicates that the lectin recognizes both N-acetylneuraminic acid and galactose-terminating biantennary oligosaccharide structures. Lectin activity is independent of calcium and appears to reside in a Mr 17,000 intracellular membrane pr...

Journal: :Veterinary Science Development 2013

Journal: :Cancer research 1985
Y Ohkuma H Komano S Natori

The binding proteins for Sarcophaga lectin and wheat germ agglutinin on the surface of Ehrlich ascites tumor cells were compared. Studies with antibody against the binding protein for Sarcophaga lectin showed that these two binding proteins are different. Since these two lectins are both active in the lectin-dependent macrophage-mediated cytotoxic reaction with Ehrlich ascites tumor cells as ta...

Journal: :Nephrology Dialysis Transplantation 2007

Journal: :FEMS Microbiology Letters 1979

Journal: :Journal of Experimental Medicine 2004

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