Soluble lactose-binding vertebrate lectins: a growing family.
Extracts of rat intestine contain nine soluble lactose-binding lectins with subunit molecular weights ranging from 14,500 to 19,000 that were purified by affinity chromatography and ion-exchange chromatography. Two of them are either identical with or closely related to other known rat lectins. A third appears to be the isolated carbohydrate-binding C-terminal domain of a known lectin but lacks the N-terminal domain presumed to mediate a different function. The others have not been described previously. Among them, the major rat intestinal lectin, RI-H, and a related protein, RI-G, have N-terminal amino acid sequences with similarities to sequences found in other known rat lectins. Therefore, these results introduce new members of a growing family of these structurally homologous soluble lactose-binding proteins.
Leffler
H
H
Department of Psychiatry, Langley Porter Psychiatric Institute, University of California, San Francisco 94143.
Masiarz
F R
FR
Barondes
S H
SH
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002852:Chromatography, Ion Exchange; D007413:Intestinal Mucosa / Q000378:metabolism*; D007422:Intestines / Q000187:drug effects; D007785:Lactose / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008168:Lung / Q000032:analysis / Q000187:drug effects; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D012995:Solubility
D037102:Lectins; D007785:Lactose