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Res Microbiol. 1996 Nov-Dec;147(9):733-7.

Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius.

Author information

1
Institut für Biologie, Humboldt-Universität zu Berlin, Germany.

Abstract

Growth of the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius strain ATCC 27009 on maltose resulted in the increased production of a protein with apparent molecular mass of 40 kDa. By metabolic labelling with 14C-palmitic acid, the 40-kDa protein was identified as a lipoprotein. The protein exhibited maltose-binding activity at pH 3.5, as demonstrated by chromatography on cross-linked amylose. Partial amino acid sequence analysis revealed that the 40-kDa protein corresponds to the product of an open reading frame downstream from the amylase gene (amy) that displays similarity to enterobacterial maltose-binding proteins.

PMID:
9296107
[Indexed for MEDLINE]

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