ArticleThe Biochemical journal1994
Preparation and characterization of novel substrates of insulin proteinase (EC 3.4.99.45).
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Modulation of Insulin Sensitivity by Insulin-Degrading Enzyme.Biomedicines · 2021Review
- Hepatic Insulin Clearance: Mechanism and Physiology.Physiology (Bethesda, Md.) · 2019Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The specificity of insulin proteinase (EC 3.4.99.45) has been difficult to categorize using only its natural substrates. By exploiting the fact that two substrates competing for the same enzyme inhibit one another, we have found some new substrates of the insulin proteinase from porcine muscle. Two of these substrates, a tryptic fragment of BSA and a fragment of cytochrome c, have been shown to be cleaved at a single site. The albumin fragment, as well as another fragment of cytochrome c., have susceptibilities (Vmax/Km) comparable with that of insulin. In a second aspect of the study, the porcine-muscle enzyme was shown to be related to other members of its superfamily in that it was immunoprecipitated by a monoclonal antibody raised against the insulin-degrading enzyme from human red blood cells and has the same cleavage sites on insulin as has the rat skeletal-muscle insulin proteinase. We note, however, a possible discrepancy between our results and those of another group regarding the subunit size (110 kDa) of the immunoprecipitated material.
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