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http://purl.uniprot.org/citations/3830151http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3830151http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3830151http://www.w3.org/2000/01/rdf-schema#comment"A 9000-Mr protein isolated from a 60% ethanolic extract of soybean (Glycine max) seeds has been characterized and fully sequenced. The protein consists of 80 amino acid residues with four disulfide bonds. It contains a large number of hydrophobic residues and lacks methionine, phenylalanine, tryptophan, lysine and histidine residues. The protein readily crystallizes from water but is quite soluble in aqueous organic solvents like 95% 1-propanol. It aggregates to form large molecules (above 80 kDa) under ordinary denaturing conditions, such as 6 M guanidine X HCl and 8 M urea. Sequence analysis showed that the amino-terminal four-fifths is extremely hydrophobic and most of the acidic residues exist as their amide forms, and only the carboxyl-terminal short segment is rather hydrophilic. A computer search for homology detected an unexpected similarity of this protein to rat prolactin; however, its significance could not be assessed and this protein appears to represent a hitherto unknown protein family. Although no biochemical activity could be detected, the existence in relatively high abundance (approx. 200 mg from 1 kg seeds) of this novel protein may suggest its physiological significance in the plant."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1987.tb10666.x"xsd:string
http://purl.uniprot.org/citations/3830151http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1987.tb10666.x"xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Koide T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Koide T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Ono T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Ono T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Odani S."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Odani S."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Tanaka T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Tanaka T."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Seto Y."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/author"Seto Y."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/pages"485-491"xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/pages"485-491"xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/title"Soybean hydrophobic protein. Isolation, partial characterization and the complete primary structure."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/title"Soybean hydrophobic protein. Isolation, partial characterization and the complete primary structure."xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/volume"162"xsd:string
http://purl.uniprot.org/citations/3830151http://purl.uniprot.org/core/volume"162"xsd:string