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Comparative specificity of microbial acid proteinases for synthetic peptides. I. Primary specificity
Authors:T Oka  K Morihara
Institution:Shionogi Research Laboratory, Shionogi & Co., Ltd., Fukushima-ku, Osaka 553, Japan
Abstract:The specificity of various acid proteinases from mold and yeast such as Aspergillus niger, Aspergillus saitoi, Rhizopus chinensis, Mucor miehei, Rhodotorula glutinis, and Cladosporium sp. were comparatively determined using with
/></figure> (X = various amino acid residues) as substrates. Pepsin was used in a comparative study. Since the peptides were susceptible to these enzymes at the peptide bonds indicated by the arrows, except for the ones from both <em>Aspergillus</em> species and <em>Rhodotorula</em>, we could examine their specificity with respect to the amino acid residue on both sides of the splitting point. The results indicated that the microbial enzymes were specific for aromatic, or bulky and hydrophobic amino acid residues on both sides, as had been observed with pepsin. The specificity of the enzymes from <em>Aspergillus</em> and <em>Rhodotorula</em> was not determined because of lack of hydrolysis of the peptides.</td> </tr> <tr> <td align=
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