Results 201 to 210 of about 23,292 (261)
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Neuropeptide-processing carboxypeptidases
Life Sciences, 2003Neuropeptides are generally produced from precursor proteins by selective cleavage at specific sites, usually involving basic amino acids. Enzymes such as the prohormone convertases and carboxypeptidase E are highly specific for these basic amino acid-containing sites.
Suwen, Wei +3 more
openaire +2 more sources
2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
openaire +2 more sources
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
openaire +2 more sources
Pig Platelet Acidic Carboxypeptidases
Enzyme and Protein, 1994Pig platelet acidic carboxypeptidases hydrolyzed only N-blocked dipeptides with bulky aromatic and aliphatic hydrophobic amino acids. The optimum hydrolysis of these substrates was at pH 5.0. The main acidic carboxypeptidase in pig platelet lysate was lysosomal carboxypeptidase A (1CPA), which hydrolyzed Cbz-Phe-Ala at the highest rate.
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Biokhimiia (Moscow, Russia), 1984
Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
openaire +1 more source
Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
openaire +1 more source
Functional segregation and emerging role of cilia‐related cytosolic carboxypeptidases (CCPs)
The FASEB Journal, 2013Mónica Rodríguez de la Vega Otazo +4 more
semanticscholar +1 more source
Applied Biochemistry and Biotechnology, 2011
Jing Fu, Li Li, Xiaoquan Yang
semanticscholar +1 more source
Jing Fu, Li Li, Xiaoquan Yang
semanticscholar +1 more source

