Leucine aminopeptidase from bovine lens and hog kidney. Comparison using immunological techniques, electron microscopy, and X-ray diffraction.
Open Access
- 1 December 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (23) , 14757-14761
- https://doi.org/10.1016/s0021-9258(17)42667-6
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Solvent content of protein crystalsPublished by Elsevier ,2006
- Effect of cryosolvents and subzero temperatures on the hydrolysis of L-leucine-p-nitroanilide by porcine kidney leucine aminopeptidaseBiochemistry, 1982
- The effect of a single amino acid substitution on the antigenic specificity of the loop region of lysozymeMolecular Immunology, 1980
- Leucine aminopeptidase (bovine lens): an electron microscopic studyJournal of Ultrastructure Research, 1979
- Amino acid sequence of California quail lysozyme. Effect of evolutionary substitutions on the antigenic structure of lysozymeBiochemistry, 1979
- Further studies of an anomalous cross-reaction involving worm and vertebrate lysozymesImmunochemistry, 1978
- Evolutionary changes ofα-crystallin and the phylogeny of mammalian ordersJournal of Molecular Evolution, 1977
- Biochemical EvolutionAnnual Review of Biochemistry, 1977
- Preliminary X-ray study of leucine aminopeptidase (bovine lens), an oligomeric metalloenzymeJournal of Molecular Biology, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970