New chloride-activated aminopeptidase from human erythrocytes
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)80934-2/fullpdf
Reference16 articles.
1. Mammalian Proteases: A Glossary and Bibliography;McDonald,1986
2. Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: Aminopeptidase B
3. Effect of Cl− on the function of the Cl−-activated arginine aminopeptidase purified from human erythrocytes
4. Substrate specificities of Cl−-activated arginine aminopeptidases from human and rat origin
5. Purification and characterization of two Cl--activated aminopeptidases hydrolysing basic termini from human skeletal muscle
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1. Characterization of the proteolytic enzymes in the midgut of the European Cockchafer, Melolontha melolontha (Coleoptera: Scarabaeidae);Insect Biochemistry and Molecular Biology;2002-07
2. Reducing Extracellular Cl− Suppresses Dihydropyridine-Sensitive Ca2+ Currents and Synaptic Transmission in Amphibian Photoreceptors;Journal of Neurophysiology;1997-04-01
3. Use of azidobestatin as a photoaffinity label to identify the active site peptide of leucine aminopeptidase;Biochemistry;1992-04-28
4. Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes;Biological Chemistry Hoppe-Seyler;1992-01
5. Types and localization of aminopeptidases in different human blood cells;International Journal of Biochemistry;1991-01
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