Literature DB >> 2430952

N-terminal sequence of soybean beta-amylase.

B Mikami, K Nomura, Y Morita.   

Abstract

The blocked N-terminus and N-terminal sequence of soybean beta-amylase were determined by analyzing the acidic peptides derived on peptic digestion of the enzyme. The acidic peptides were separated from the digest on a Dowex 50 X 2 column and purified by reversed phase-high performance liquid chromatography (RP-HPLC). The major acidic peptide, Pep-4, was a heptapeptide with a molecular weight of 766. Forty-eight hundredths mol acetyl group and 0.61 mol acetyl-Ala per mol of Pep-4 were detected on RP-HPLC analysis. The N-terminal 9 amino acid sequence of soybean beta-amylase was deduced to be acetyl-Ala-Thr-Ser-Asp-Ser-Asn-Met-(Gly-Leu) from the results of sequence analysis of Pep-4 and amino acid analysis of other acidic peptides.

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Year:  1986        PMID: 2430952     DOI: 10.1093/oxfordjournals.jbchem.a121741

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  1 in total

1.  Characterization of a maize beta-amylase cDNA clone and its expression during seed germination.

Authors:  S M Wang; W L Lue; S Y Wu; H W Huang; J Chen
Journal:  Plant Physiol       Date:  1997-02       Impact factor: 8.340

  1 in total

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