The Amino Acid Sequence of Goatß-Lactoglobulin

Autor: Gisèle Préaux, Schrank B, A Stangl, Gerhard Braunitzer
Rok vydání: 1979
Předmět:
Zdroj: Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 360:1595-1604
ISSN: 0018-4888
DOI: 10.1515/bchm2.1979.360.2.1595
Popis: The isolation of beta-lactoglobulin from milk of the goat is described. The purified protein was checked for purity and has been characterized by its gross composition and end groups. The native or the modified protein was then degraded by tryptic and cyanogen bromide cleavage. The cleavage products were isolated and sequenced in the sequenator using a Quadrol and propyne program. These data provide the complete sequence of beta-lactoglobulin of the goat. The results are discussed and compared particularly with bovine beta-lactoglobulin components AB. Some biological aspects are described.
Databáze: OpenAIRE