نتایج جستجو برای: lectin

تعداد نتایج: 15656  

Journal: :Cellular immunology 1982
D E Maddox I J Goldstein A F Lobuglio

The concurrent administration of Griffonia simplicifolia lectin into the peritoneal cavity of mice has been reported to protect them from challenge with Ehrlich ascites tumor cells. This study demonstrates that the GS I lectin is capable of binding to the surface of both inflammatory macrophages and Ehrlich ascites tumor cells and can mediate macrophage lectin-dependent cytotoxicity to this tum...

2016
Lei Zhang Shen Luo Baolin Zhang

Glycans or carbohydrates attached to therapeutic glycoproteins can directly affect product quality, safety and efficacy, and therefore must be adequately analyzed and controlled throughout product life cycles. However, the complexity of protein glycosylation poses a daunting analytical challenge. In this study, we evaluated the utility of a lectin microarray for assessing protein glycans. Using...

2007
Prapaporn Utarabhand Wanida Rittidach Nisa Paijit

A lectin from the hemolymph of the banana shrimp Penaeus (Fenneropenaeus) merguiensis expressed higher agglutination activity against rabbit erythrocytes than those from human, and its activity was Cadependent. The hemagglutinating activity of the hemolymph lectin was stable up to 55 C and optimal at pH 7.5-8.0. N-acetylated sugars, ManNAc, GlcNAc, GalNAc, and NeuNAc, were effective inhibitors ...

Journal: :The Journal of biological chemistry 1988
K Yamashita K Umetsu T Suzuki Y Iwaki T Endo A Kobata

The carbohydrate binding specificity of Allomyrina dichotoma lectin II was investigated by analyzing the behavior of various complex type oligosaccharides and human milk oligosaccharides on an A. dichotoma lectin II-agarose column. Basically, the lectin interacts with the Gal beta 1----4GlcNAc group. Substitution of their terminal galactose residues by Neu5Ac alpha 2----6 will enhance their aff...

Journal: :Preparative biochemistry & biotechnology 1999
P Hernández M Bacilio F Porras S Juarez H Debray E Zenteno B Ortiz

Amaranthus leucocarpus lectin is a homodimeric glycoprotein of 35 kDa per sub-unit, which interacts specifically with N-acetyl-galactosamine. In this work, we compared different glycoproteins that contain Galbeta1-3 GalNAcalpha1-3 Ser/Thr or GalNAcalpha1-3 Ser/Thr in their structure as ligands to purify the A. leucocarpus lectin. From the glycoproteins tested, fetuin was the most potent inhibit...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Misao Matsushita Akiko Matsushita Yuichi Endo Munehiro Nakata Naoya Kojima Tsuguo Mizuochi Teizo Fujita

The lectin complement pathway in innate immunity is closely related to the classical complement pathway in adaptive immunity, with respect to the structures and functions of their components. Both pathways are initiated by complexes consisting of collagenous proteins and serine proteases of the mannose-binding lectin (MBL)-associated serine protease (MASP)/C1r/C1s family. It has been speculated...

Journal: :Journal of immunology 2006
Momoe Takahashi Daisuke Iwaki Akiko Matsushita Munehiro Nakata Misao Matsushita Yuichi Endo Teizo Fujita

The recognition of pathogens is mediated by a set of pattern recognition molecules that recognize conserved pathogen-associated molecular patterns shared by broad classes of microorganisms. Mannose-binding lectin (MBL) is one of the pattern recognition molecules and activates complement in association with MBL-associated serine protease (MASP) via the lectin pathway. Recently, an MBL-like lecti...

Journal: :The Biochemical journal 2006
Takahiro Tanji Ayako Ohashi-Kobayashi Shunji Natori

A galactose-specific C-type lectin has been purified from a pupal extract of Drosophila melanogaster. This lectin gene, named DL1 (Drosophila lectin 1), is part of a gene cluster with the other two galactose-specific C-type lectin genes, named DL2 (Drosophila lectin 2) and DL3 (Drosophila lectin 3). These three genes are expressed differentially in fruit fly, but show similar haemagglutinating ...

Journal: :Journal of nutritional science and vitaminology 1984
T Hara Y Mukunoki I Tsukamoto M Miyoshi K Hasegawa

The enzymatic digestion of a Kintoki bean lectin in vitro resulted in neither the extensive hydrolysis nor complete inactivation of the lectin. The majority of [3H]lectin administered to mice by stomach-intubation was found in the digestive tract at levels of 88.7%, 99.4%, 99.5% and 78.6%, after 0.5, 2, 5 and 24h of intubation, respectively. Twenty to forty percent of the administered radioacti...

Journal: :The Journal of biological chemistry 1977
T P Nowak D Kobiler L E Roel S H Barondes

A lectin, whose specific activity in soluble extracts of embryonic chick pectoral muscle increases strikingly between 8 and 16 days of development, has been purified by affinity chromatography on derivatized Sepharose 4B coupled to p-aminophenyl-beta-D-lactoside. After affinity chromatography the lectin is pure except for minor contamination with another protein possibly representing a second m...

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