Isolation of lectin and albumin from Pisum sativum var. macrocarpon ser. cv. sugar snap.
A mannose- and glucose-binding lectin bearing considerable sequence similarity to other legume lectins was isolated using a simple procedure, from legumes of the sugar snap Pisum sativum var. macrocarpon. The lectin was unadsorbed on Affi-gel blue gel and Q-Sepharose in 10 mM Tris-HCl buffer (pH 7.2) and adsorbed on SP-Toyopearl in 50 mM NaOAc buffer (pH 5). An albumin could also be purified at the same time. It was unadsorbed on Affi-gel Blue gel, adsorbed on Q-Sepharose and unadsorbed on SP-Toyopearl under the aforementioned chromatographic conditions. The lectin was almost identical in N-terminal sequences of its alpha- and beta-subunit to lectin from P. sativum L. var. Feltham First except for the 19th N-terminal residue of the beta-subunit. The lectin was devoid of antifungal activity. Out of the 15 N-terminal amino acids examined in pea albumin, three were different between the two varieties of P. sativum.
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Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong, China.
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D000418:Albumins / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006388:Hemagglutinins / Q000378:metabolism; D037102:Lectins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000737:chemistry*; D037121:Plant Lectins; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D000418:Albumins; D006388:Hemagglutinins; D037102:Lectins; D037121:Plant Lectins; D012333:RNA, Messenger