The influence of chronic ethanol feeding to rats on the integrity of liver mitochondrial membrane as assessed with the Mg2+-stimulated ATPase enzyme. |
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Authors: | E A Hosein I Hofmann E Linder |
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Affiliation: | 1. Department of Microbiology, New York University School of Medicine, New York, New York 10016 U.S.A.;2. Department of Biochemistry, New York University School of Medicine, New York, New York 10016 U.S.A.;3. Department of Medicine, New York University School of Medicine, New York, New York 10016 U.S.A.;4. Department of Pathology, New York University School of Medicine, New York, New York 10016 U.S.A.;5. The Irvington House Institute for Medical Research U.S.A. |
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Abstract: | The mouse submaxillary proteases (A + D), the isolation and properties of which were previously described by us, hydrolyze only arginyl bonds in proteins. Formol titrations and peptide mapping on digests of polyarginine, polylysine, lysozyme, histone, and insulin suggested this specificity. Amino acid compositions of peptides from lysozyme and insulin showed that most but not all arginyl bonds were hydrolyzed but that no lysyl bonds were split. The proteases should be useful in the sequencing of proteins. |
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