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Literature DB >> 4595280

Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A.

Abstract

The amino acid sequence of subunit A of the potato chymotryptic inhibitor I was determined. The sequence was deduced from analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide, N-bromosuccinimide and dilute acid, and by digestion with trypsin, thermolysin, pepsin and papain. The molecule consists of a single polypeptide chain of 84 residues, which contains two homologous regions each of 13 amino acids. The protein does not appear to be homologous with any other known proteinase inhibitors.

Entities: Chemical Species

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Substances：

Year: 1974 PMID： 4595280 PMCID： PMC1166086 DOI： 10.1042/bj1370101

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

30 in total

1. SIMPLIFIED "DISC" (POLYACRYLAMIDE GEL) ELECTROPHORESIS.

Authors: J T CLARKE
Journal: Ann N Y Acad Sci Date: 1964-12-28 Impact factor: 5.691

2. Chemical and physicochemical characterization of potato proteinase inhibitor I and comparison of its specificity with those of inhibitors II-a and II-b.

Authors: T Kiyohara; T Iwasaki; M Yoshikawa
Journal: J Biochem Date: 1973-01 Impact factor: 3.387

3. [On plant protease inhibitors. V. Isolation and characterization of some polyvalent protease inhibitors from Solanum tuberosum].

Authors: K Hochstrasser; E Werle; R Siegelmann; S Schwarz
Journal: Hoppe Seylers Z Physiol Chem Date: 1969-07

4. Isolation of three isoinhibitors of trypsin from garden bean, Phaseolus vulgaris, having either lysine or arginine at the reactive site.

Authors: K A Wilson; M Laskowski
Journal: J Biol Chem Date: 1973-02-10 Impact factor: 5.157

3. Sequence of the amino-terminal part of enterotoxin from Clostridium perfringens type A: identification of points of trypsin activation.

Authors: M Richardson; P E Granum
Journal: Infect Immun Date: 1983-06 Impact factor: 3.441

3 in total

Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A.

1. SIMPLIFIED "DISC" (POLYACRYLAMIDE GEL) ELECTROPHORESIS.

2. Chemical and physicochemical characterization of potato proteinase inhibitor I and comparison of its specificity with those of inhibitors II-a and II-b.

3. [On plant protease inhibitors. V. Isolation and characterization of some polyvalent protease inhibitors from Solanum tuberosum].

4. Isolation of three isoinhibitors of trypsin from garden bean, Phaseolus vulgaris, having either lysine or arginine at the reactive site.

5. Chymotrypsin inhibitor I from potatoes: reactivity with mammalian, plant, bacterial, and fungal proteinases.

6. Repeating sequences and gene duplication in proteins.

7. The amino acid sequence of soybean trypsin inhibitor (Kunitz).

8. The amino-acid sequence of the cytochrome c of Ginkgo biloba L.

9. Identification of the trypsin-reactive site of the Bowman-Birk soybean inhibitor.

10. Isolation of a carboxypeptidase B inhibitor from potattoes.

1. The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding sequence for preprovicilin.

2. Evidence for the presence of proteinase inhibitor I in vacuolar protein bodies of plant cells.

3. Sequence of the amino-terminal part of enterotoxin from Clostridium perfringens type A: identification of points of trypsin activation.