An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I
| ISSN: |
1573-4943
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| Keywords: |
Insulin analogue ; insulin-like-growth factor ; peptide synthesis ; receptor binding assay ; lipogenesis
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Chemistry and Pharmacology
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| Notes: |
Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798296778335846404 |
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| autor | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| autorsonst | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| book_url | http://dx.doi.org/10.1007/BF01025314 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM197817270 |
| issn | 1573-4943 |
| journal_name | The protein journal |
| materialart | 1 |
| notes | Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors. |
| package_name | Springer |
| publikationsjahr_anzeige | 1990 |
| publikationsjahr_facette | 1990 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1990 |
| publisher | Springer |
| reference | 9 (1990), S. 235-246 |
| schlagwort | Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis |
| search_space | articles |
| shingle_author_1 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_2 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_3 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_4 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_catch_all_1 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors. 1573-4943 15734943 Springer |
| shingle_catch_all_2 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors. 1573-4943 15734943 Springer |
| shingle_catch_all_3 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors. 1573-4943 15734943 Springer |
| shingle_catch_all_4 | Joshi, Satish Burke, G. Thompson Katsoyannis, Panayotis G. An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Insulin analogue insulin-like-growth factor peptide synthesis receptor binding assay lipogenesis Abstract We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors. 1573-4943 15734943 Springer |
| shingle_title_1 | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| shingle_title_2 | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| shingle_title_3 | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| shingle_title_4 | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:57:30.092Z |
| titel | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| titel_suche | An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I |
| topic | V |
| uid | nat_lic_papers_NLM197817270 |