concanavalin-a and laminaran

concanavalin-a has been researched along with laminaran* in 1 studies

Other Studies

1 other study(ies) available for concanavalin-a and laminaran

Article	Year
Purification and comparison of beta-1,3-glucan binding protein from white shrimp (Penaeus vannamei). Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 1997, Volume: 116, Issue:4 A beta-glucan binding protein (BGBP) was identified in both white (Penaeus vannamei) and blue shrimp (P. stylirostris) plasma. White shrimp BGBP was purified by affinity chromatography using immobilized laminarin, and its molecular and biological properties were described. White shrimp BGBP is a monomeric protein with a molecular mass of 100 kDa, similar to those described for other crustacean BGBPs. White and blue shrimp BGBPs can be detected with antisera against crayfish BGBP and brown shrimp BGBP. Both amino acid composition and N-terminal sequence are markedly similar to brown shrimp (P. californiensis) and crayfish (Pacifastacus leniusculus) BGBP, indicating that this recognition protein is present in freshwater and marine crustaceans. Topics: Agglutinins; Amino Acid Sequence; Amino Acids; Animals; Astacoidea; Carrier Proteins; Chromatography, Liquid; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Glucans; Glycosylation; Lectins; Mice; Molecular Sequence Data; Molecular Weight; Penaeidae; Polysaccharides; Sequence Homology, Amino Acid	1997

Article

Year

Purification and comparison of beta-1,3-glucan binding protein from white shrimp (Penaeus vannamei).

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 1997, Volume: 116, Issue:4

A beta-glucan binding protein (BGBP) was identified in both white (Penaeus vannamei) and blue shrimp (P. stylirostris) plasma. White shrimp BGBP was purified by affinity chromatography using immobilized laminarin, and its molecular and biological properties were described. White shrimp BGBP is a monomeric protein with a molecular mass of 100 kDa, similar to those described for other crustacean BGBPs. White and blue shrimp BGBPs can be detected with antisera against crayfish BGBP and brown shrimp BGBP. Both amino acid composition and N-terminal sequence are markedly similar to brown shrimp (P. californiensis) and crayfish (Pacifastacus leniusculus) BGBP, indicating that this recognition protein is present in freshwater and marine crustaceans.

Topics: Agglutinins; Amino Acid Sequence; Amino Acids; Animals; Astacoidea; Carrier Proteins; Chromatography, Liquid; Concanavalin A; Electrophoresis, Polyacrylamide Gel; Glucans; Glycosylation; Lectins; Mice; Molecular Sequence Data; Molecular Weight; Penaeidae; Polysaccharides; Sequence Homology, Amino Acid

1997