Hormonal and immunological properties of insulin fragments. II. Products obtained by enzymatic hydrolysis
| Autor: | Guillermo Lucena, Barbara Surmaczynska, Robert Metz, Richard J. Barrett |
|---|---|
| Rok vydání: | 1969 |
| Předmět: |
medicine.medical_specialty
Swine medicine.medical_treatment Insulin Antibodies Diaphragm Guinea Pigs Carboxypeptidases Fat pad Drug Hypersensitivity Residue (chemistry) Endocrinology Enzymatic hydrolysis Internal medicine medicine Animals Humans Insulin Trypsin chemistry.chemical_classification Immunoassay biology Immunoglobulin E Carboxypeptidase Amino acid Biochemistry chemistry Adipose Tissue biology.protein Chromatography Gel Biological Assay Cattle Digestion Peptides medicine.drug |
| Zdroj: | Endocrinology. 85(3) |
| ISSN: | 0013-7227 |
| Popis: | Beef insulin was subjected to tryptic digestion to obtain desoctapeptide insulin (removal of the C-terminal 8 amino acid residues of the B-chain) and to carboxypeptidase digestion to obtain desalanine-desasparagine insulin (removal of the C-terminal residue from each chain). Both fragments appeared to be inertwhen tested for insulin-like activity on rat diaphragm and rat fat pad assays and both seemed to have lost the capacity to interact with “insulin-neutralizing” antisera. However, both fragments were apparently capable of reacting with a human reaginic antibody to insulin. (Endocrinology 85: 577, 1969) |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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