Studies on the Components of Mammalian Urine |
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| Authors: | Rikisaku Suemitsu Shin-ichi Fujita Mitsuo Yoshimura Hogyoku Gen Akira Yuasa Jun-ichi Ushijima |
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| Affiliation: | 1. Department of Applied Chemistry, Faculty of Engineering, Doshisha University, Kamikyo-ku, Kyoto;2. Rakuno College, Nopporo, Ebetsu, Hokkaido |
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| Abstract: | Pectate lyase was purified approximately 29-fold to electrophoretic homogeneity from Pseudomonas marginalis N6301. A pectate lyase (PL; EC4.2.2.2) gene of the strain was cloned and expressed in Escherichiacoli. The nucleotides of the PL gene (pel) were sequenced. An open reading frame that encodes a polypeptide (molecular weight: 40,812) composed of 380 amino acids including a 29 amino acid signal peptide was assigned. The structural gene of pel consisted of 1140 base pairs. The nucleotide sequence of the 5′-flanking region of pel showed a consensus sequence of the promoter region of the pectin lyase gene (pnl) in P. marginalis N6301, a Pribnow box, and a ribosome binding site as found in E. coli. |
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| Keywords: | Fusarium glycoproteins endo-β-galactofuranosidase Bacillus carbohydrate chains |
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