The conserved tryptophan-arginine-tyrosine motif of a proteinaceous α-amylase inhibitor T-76 from Streptomyces nitrosporeus is important for inhibition of animal α-amylases but not for an α-amylase from Bacillus sp. no. 195-Reference-Cited by-同舟云学术

The conserved tryptophan-arginine-tyrosine motif of a proteinaceous α-amylase inhibitor T-76 from Streptomyces nitrosporeus is important for inhibition of animal α-amylases but not for an α-amylase from Bacillus sp. no. 195

Published:2000-01 Issue:1 Volume:90 Page:74-80
ISSN:1389-1723
Container-title:Journal of Bioscience and Bioengineering
language:en
Short-container-title:Journal of Bioscience and Bioengineering

Author:

Sumitani Jun-Ichi,Hattori Noriaki,Nakamura Yuri,Okuda Yasuhisa,Kawaguchi Takashi,Arai Motoo

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Reference27 articles.

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2. Primary structure of Paim I, an α-amylase inhibitor from Streptomyces crochorusii, determined by the combination of Edman degradation and fast atom bombardment mass spectrometry;Hirayama;Biochemistry,1987

3. Molecular cloning and expression of proteinaceous α-amylase inhibitor gene from Streptomyces nitrosporeus;Sumitani;Biosci. Biotech. Biochem.,1993

4. New proteinaceous α-amylase inhibitor (N-61) from Streptomyces viridochromogenes;Nishimura;Chem. Express,1991

5. Die sequenz des α-amylase inhibitors HOE 467 A (α-amylase-inactivator HOE 467 A) aus Streptomyces tendae 4158;Aschauser;Hoppe-Seyler's Z. Physiol. Chem.,1981

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