• Publications
  • Influence
Enterokinase (enteropeptidase): comparative aspects.
TLDR
The serine protease enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile, suggesting that enteringokinase lies on the same phylogenetic branch as the blood-clotting proteins. Expand
Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase.
TLDR
The cloning and functional expression of a cDNA encoding the catalytic domain (light chain) of bovine enterokinase is reported and the nucleotide sequence of this cloned cDNA predicts a 235-amino acid polypeptide that shares a high degree of homology with a variety of mammalian serine proteases involved in digestion, coagulation, and fibrinolysis. Expand
CURRENT STATUS OF THE STRUCTURE OF PAPAIN: THE LINEAR SEQUENCE, ACTIVE SULFHYDRYL GROUP, AND THE DISULFIDE BRIDGES.
[46] Partial acid hydrolysis
Publisher Summary This chapter discusses the mechanism of partial acid hydrolysis. Hydrolysis of a peptide in strong acid for short periods produces a mixture of products with free amino acids andExpand
Effect of cleaving interchain disulfide bridges on the radius of gyration and maximum length of anti-poly(D-alanyl) antibodies before and after reaction with tetraalanine hapten.
TLDR
Data from the small-angle x-ray scattering of solutions of rabbits IgG antibodies and their derivatives lend further support to the notion that binding of hapten induces a conformational transition in its specific antibodies and suggest that the opening of the interchain disulfide bridges affects that transition. Expand
Effect of corynetoxin isolated from parasitized annual ryegrass on albumin and transferrin synthesis and secretion by cultured fetal rat hepatocytes.
TLDR
The effects of CT on protein synthesis and secretion in cultured hepatocytes are similar to those reported for tunicamycin (TM), where glycosylation of the protein is not required for secretion. Expand
Proteins: structure and function
Comparative studies on the modification of specific disulfide bonds of trypsinogen and chymotrypsinogen.
TLDR
The formation of catalytically active molecules from the modified zymogen shows that the two disulfides are non-essential structural elements, and the two zymogens differ in conformation in regions of homologous sequences. Expand
CHEMICAL AND ENZYMIC STUDIES ON THE AMINO-TERMINAL SEQUENCE OF PAPAIN. A REINVESTIGATION.
TLDR
A reinvestigation of the NHz-terminal sequence of papain with highly purified leucine aminopeptidase indicated that mercuripapain is not significantly degraded by the enzyme. Expand
[20] Leucine aminopeptidase in sequence determination of peptides.
  • A. Light
  • Chemistry, Medicine
  • Methods in enzymology
  • 1972
TLDR
The tryptic digest, without further separation, is submitted to hydrolysis by LAP, which released amino acids exclusively from the newly exposed glutamine sequence. Expand
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