RS Singh, R Bhari, HP Kaur - Critical reviews in biotechnology, 2011 - Taylor & Francis
Lectins are widespread in nature and have been isolated from plants, animals, microorganisms, and viruses. Although several lectins have been reported from microfungi …
A novel lectin was purified from newly cyanobacterium isolate, Oscillatoria acuminate MHM- 632 MK014210. 1 using affinity chromatography with a molecular weight of 120 kDa under …
Background Lectins are carbohydrate binding proteins or glycoproteins that bind reversibly to specific carbohydrates present on the apposing cells, which are responsible for their …
RS Singh, HP Kaur, J Singh - Process Biochemistry, 2015 - Elsevier
A lectin was isolated from Aspergillus panamensis mycelia using single-step affinity chromatography on porcine stomach mucin coupled Sepharose 4B. A purification fold of …
Lectins bind to surface receptors on target cells, and activate a cascade of events, eventually leading to altered immune status of host. The immunomodulatory potential of purified lectin …
KM Barakat, YM Gohar - Indian journal of microbiology, 2012 - Springer
Screening of fungal isolates collected from different locations of Alexandria coast, Egypt, was carried out to obtain new biologically active metabolites against some virulent fish …
RS Singh, R Bhari, R Kaur - Applied biochemistry and biotechnology, 2015 - Springer
Lectins are carbohydrate binding proteins or glycoproteins that bind reversibly to specific carbohydrates present on the apposing cells, which is responsible for their ability to …
Mucin-specific lectin from mycelium of Aspergillus nidulans was purified using anion exchange and gel filtration chromatographic techniques with an overall recovery of 32% and …
Lectin activity was assessed in sixteen Aspergillius species using human A, B, O, AB, rabbit, goat, pig and sheep erythrocytes. Neuraminidase and protease treated blood group O …