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Microanalysis of the Amino-Acid Sequence of Monomeric β-Lactoglobulin I from Donkey (Equus asinus) milk. The Primary Structure and its Homology with a Superfamily of Hydrophobic Molecule Transporters by Jasminka GODOVAC-ZIMMERMANN; Amedeo CONTI; Lewis JAMES; Lorenzo NAPOLITANO is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The complete primary structure of donkey ß-lactoglobulin I was determined by pulsed-liquid phase microsequeincing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric ß-lactoglobulin of type I.. With the inclusion of donkey ß-lactoglobudin I there are 13% common residues amongstt the members of the ß-lactoglobulin family. Donkey ß-lactoglobulin I is homologous to the retinol-bindng protein, bilin-binding protein and five otherproteins belonging to the new superfamily of h/drophobic molecule transporters. A rapid rrethod for peptide isolation and the strategy for micro sequencing of this protein have been described. ## Mikroanalyse der Aminosäures&quenz des monomeren ß-Lactoglobulins I aus Eselsmilch (Equus asinus): Die PrimärstruJktur und ihre Homologie mit einer Überfamilie hydrophober Transportmoleküüe Zusammenfassung: Die vollständige Primärstruktur vom ß-Lactoglobulin I des Esels wurde mittels Pulsations-Flüssigphasen-Miikrosequenzierung der tryptischen Peptide bestimmt. Das Protein wurde in monomerer Fcorm erhalten und es entspricht monomerem /ß-Lactoglobulin vom Typ L Die Proteinsequenzen der ß-Lactoglobulin-Familie (einschließl

Who reads Microanalysis of the Amino-Acid Sequence of Monomeric β-Lactoglobulin I from Donkey (Equus asinus) milk. The Primary Structure and its Homology with a Superfamily of Hydrophobic Molecule Transporters?

Author

Jasminka GODOVAC-ZIMMERMANN; Amedeo CONTI; Lewis JAMES; Lorenzo NAPOLITANO

Published

1988

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)