The isolation and partial characterization of trypsinogen, pancreatic secretory trypsin inhibitor and multiple forms of chymotrypsinogen and trypsin from the pancreas of the ostrich (Struthio camelus)
| Autor: | Claude Lazure, András Patthy, Willem Oelofsen, Ryno J. Naudé, Nanette Smith |
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| Rok vydání: | 1992 |
| Předmět: |
Trypsinogen
Molecular Sequence Data Chymotrypsinogen Biology Biochemistry Chromatography Affinity Birds chemistry.chemical_compound PstI Affinity chromatography Sequence Homology Nucleic Acid medicine Animals Humans Trypsin Amino Acid Sequence Amino Acids Pancreatic Secretory Trypsin Inhibitor Pancreas chemistry.chemical_classification Chromatography Amino acid chemistry Pancreatic juice biology.protein Chromatography Gel Trypsin Inhibitors medicine.drug |
| Zdroj: | The International journal of biochemistry. 24(6) |
| ISSN: | 0020-711X |
| Popis: | 1. 1. PSTI, two chymotrypsinogens and two trypsins were purified to homogeneity by acid extraction, salt fractionation, SP-Sephadex C-50 chromatography and RP-HPLC. 2. 2. A third chymotrypsinogen, a trypsinogen and another trypsin were purified using an alkaline extraction procedure, followed by Trasylol- and Benzamidine-Sepharose affinity chromatography and hydroxylapatite chromatography. 3. 3. The enzymes differed in amino acid composition as well as in specific activities towards synthetic amidase and esterase substrates. 4. 4. N-terminal amino acid sequences were determined for one chymotrypsinogen and one trypsin. |
| Databáze: | OpenAIRE |
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