Document Detail

Isolation, partial characterisation, and amino acid sequence of alpha-lactalbumin from platypus (Ornithorhynchus anatinus) milk.
MedLine Citation:
PMID:  8431467     Owner:  NLM     Status:  MEDLINE    
alpha-Lactalbumin was isolated from the whey fraction of platypus (Ornithorhynchus anatinus) milk by successive ion-exchange, hydrophobic interaction and gel-permeation chromatography. The purified protein modified the action of partially-purified galactosyltransferase from platypus milk to promote the synthesis of lactose, but had very little modifier effect on bovine galactosyltransferase. Platypus alpha-lactalbumin has 126 amino-acid residues (molecular mass about 14.3 kDa), including a three-residue insertion not found in other alpha-lactalbumins or c-type lysozymes. It appears to have two sites of post-translational modification, of which at least one is N-glycosylated, to give an apparent molecular mass of 23 kDa on SDS-PAGE. The platypus sequence shows a high degree of positional identity (41-48%) with the alpha-lactalbumins of other species. Although it has no lysozyme activity, platypus alpha-lactalbumin is more similar to mammalian lysozymes than is any eutherian or marsupial alpha-lactalbumin, suggesting that this monotreme protein has evolved more slowly than other alpha-lactalbumins.
D C Shaw; M Messer; A M Scrivener; K R Nicholas; M Griffiths
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1161     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1993 Feb 
Date Detail:
Created Date:  1993-03-16     Completed Date:  1993-03-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  177-86     Citation Subset:  IM    
Protein Biochemistry Group, John Curtin School of Medical Research, Australian National University, Canberra.
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MeSH Terms
Amino Acid Sequence
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Lactalbumin / chemistry,  isolation & purification,  metabolism*
Milk / chemistry*
Molecular Sequence Data
Sequence Homology, Amino Acid
Species Specificity
Reg. No./Substance:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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