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The carbohydrate moiety of the acid carboxypeptidase fromAspergillus saitoi

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Abstract

Acid carboxypeptidase fromAspergillus saitoi is a glycoprotein that contains both N-and O-linked sugar chains. The N-glycanase released high-mannose type oligosaccharides that were separated into eight components on HPLC. One, which had a unique structure of Man11GlcNAc2, was characterized. Mild alkali treatment of the carboxypeptidase, under conditions that effect β-elimination, yieldedd-mannose. Deglycosylation of the carboxypeptidase with endo-β-N-acetylglucosaminidase and α-mannosidase effected the reduction of the molecular mass from 72 kDa to 60 kDa. Partial changes of CD spectra of the native and the deglycosylated enzymes indicate that some conformational changes on the peptide of the enzyme occurred after deglycosylation. Other enzymatic properties, such as catalytic activity, pH, and thermal stability and resistivity to protease digestion, did not appear to change. Tunicamycin halted secretion of the carboxypeptidase extracellularly.

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Authors and Affiliations

  1. Laboratory of Molecular Enzymology, Department of Applied Biologica Chemistry, Faculty of Agriculture, Tohoku University, 1-1, Tsutsumidori-Amamiyamachi, Aobaku, Sendai, Japan

    Yasunori Chiba, Youhei Yamagata, Tasuku Nakajima &  Eiji Ichishima

  2. Department of Agricultural Chemistry, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan

    Shigeyuki Iijima

Authors
  1. Yasunori Chiba
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  2. Youhei Yamagata
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  3. Shigeyuki Iijima
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  4. Tasuku Nakajima
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  5. Eiji Ichishima
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Chiba, Y., Yamagata, Y., Iijima, S. et al. The carbohydrate moiety of the acid carboxypeptidase fromAspergillus saitoi . Current Microbiology 27, 281–288 (1993). https://doi.org/10.1007/BF01575993

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