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Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit
- Source :
- Biochemical and Biophysical Research Communications. 74:1066-1070
- Publication Year :
- 1977
- Publisher :
- Elsevier BV, 1977.
-
Abstract
- Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.
- Subjects :
- Male
Protein subunit
Biophysics
Peptide
Biology
Biochemistry
Isozyme
Mice
chemistry.chemical_compound
Species Specificity
Lactate dehydrogenase
Testis
medicine
Animals
Trypsin
Amino Acid Sequence
Molecular Biology
Peptide sequence
chemistry.chemical_classification
L-Lactate Dehydrogenase
Protein primary structure
Cell Biology
Peptide Fragments
Isoenzymes
chemistry
Cysteine
medicine.drug
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 74
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....93f339d1affa441f9eec9f20101a8fe0
- Full Text :
- https://doi.org/10.1016/0006-291x(77)91626-6