Literature DB >> 1466791

The amino-acid sequence of two isoforms of alpha-lactalbumin from donkey (Equus asinus) milk is identical.

M G Giufrida1, A Cantisani, L Napolitano, A Conti, J Godovac-Zimmermann.   

Abstract

The complete primary structure of donkey alpha-lactalbumin A and B has been determined by sequencing of the peptides obtained after tryptic, Glu-C proteinase or cyanogen bromide cleavage. Although preparative purification of alpha-lactalbumin by flat-bed isoelectric focusing gave two protein fractions A and B, their amino-acid sequence revealed no differences. Donkey alpha-lactalbumin shows two, four and five differences in comparison to the horse alpha-lactalbumin A, B and C. Thus donkey alpha-lactalbumin is homogeneous and belongs to the horse A-type variant.

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Year:  1992        PMID: 1466791     DOI: 10.1515/bchm3.1992.373.2.931

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  1 in total

1.  A sensitive and effective proteomic approach to identify she-donkey's and goat's milk adulterations by MALDI-TOF MS fingerprinting.

Authors:  Francesco Di Girolamo; Andrea Masotti; Guglielmo Salvatori; Margherita Scapaticci; Maurizio Muraca; Lorenza Putignani
Journal:  Int J Mol Sci       Date:  2014-08-08       Impact factor: 5.923

  1 in total

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