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
- 1 January 1988
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 369 (1), 171-180
- https://doi.org/10.1515/bchm3.1988.369.1.171
Abstract
The complete primary structure of donkey .beta.-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric .beta.-lactoglobulin of type I. With the inclusion of donkey .beta.-lactoglobulin I there are 13% common residues amongst the members of the .beta.-lactoglobulin family. Donkey .beta.-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporter. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.This publication has 27 references indexed in Scilit:
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