Comparative biochemical analysis of lectin and nuclease from Chelidonium majus L.
It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Goździcka-Józefiak & Kedzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24 kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.
Fik
E
E
Institute of Molecular Biology and Biotechnology, Poznań, Poland.
Dalgalarrondo
M
M
Haertlé
T
T
Goździcka-Józefiak
A
A
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003851:Deoxyribonucleases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D006386:Hemagglutination Tests; D006801:Humans; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D008969:Molecular Sequence Data; D010207:Papaver / Q000737:chemistry* / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry; D018515:Plant Leaves; D037121:Plant Lectins; D018517:Plant Roots; D010946:Plants, Medicinal
D006023:Glycoproteins; D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; D003851:Deoxyribonucleases