Results 231 to 240 of about 24,475 (262)
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Crystallization of mouse pancreatic ribonuclease
Journal of Molecular Biology, 1988Mouse pancreatic ribonuclease has been crystallized in a form suitable for X-ray structure determination. The crystals grown from solutions of 2-methyl-2,4-pentanediol diffract to high resolution and belong to the hexagonal space group P6(1) (P6(5)) with unit cells dimensions a = b = 64.44 A, c = 53.91 A, y = 120 degrees and V = 1.94 x 10(5) A3 (1 A ...
A L, Perry, R A, Palmer
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The return of pancreatic ribonucleases
Trends in Biochemical Sciences, 1989A decade after losing favor as an 'uninteresting' digestive enzyme, pancreatic ribonuclease has been found to be homologous to a series of extracellular proteins that may influence tumor cell growth, neurological development and biological differentiation.
S A, Benner, R K, Allemann
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Immunologic comparison of pancreatic ribonucleases
Immunochemistry, 1976Abstract Ouchterlony double immunodiffusion and micro-complement fixation were used in cross-reactivity studies with 9 pancreatic ribonucleases differing 3–28% in amino acid sequence and rabbit antisera to cow, gnu, reindeer and whale ribonuclease.
WELLING, Gjalt W. +4 more
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Ribonuclease of bovine milk: Serological relationship to pancreatic ribonuclease
Archives of Biochemistry and Biophysics, 1964Abstract Ribonuclease isolated from bovine milk has been shown to be serologically identical to pancreatic ribonuclease. The presence of ribonuclease in milk was demonstrated directly by a gel-diffusion method. The serological method employed did not detect ribonuclease in bovine serum.
E J, COULSON, H, STEVENS
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Semisynthetic studies on bovine pancreatic ribonuclease
International Journal of Peptide and Protein Research, 1984The S‐peptide of the enzyme bovine pancreatic ribonuclease has been used as a model for covalent semisynthesis. Methods for side‐chain protection, enzymatic cleavage of the peptide chain at the level of the single arginine‐10 and for selective deprotection of the α‐carboxyl function of this residue, have been examined.
C, Di Bello +3 more
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The molecular evolution of pancreatic ribonuclease
Journal of Molecular Evolution, 1977The primary structures of pancreatic ribonucleases from 26 species (18 artiodactyls, horse, whale, 5 rodents and turtle) are known. Several species contain identical ribonucleases (cow/bison; sheep/goat), other species show polymorphism (arabian camel) or the presence of two structural gene loci (guinea pig pancreas contains two ribonucleases that ...
Beintema, Jaap J. +4 more
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Biological Function of Pancreatic Ribonuclease
Nature, 1969The physiological function of this much studied pancreatic enzyme has been misunderstood. It is essential only in ruminants and certain other herbivores, where it has a special function.
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Nucleotide sequence encoding human pancreatic ribonuclease
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1994A cDNA coding for human pancreatic ribonuclease was isolated from a pancreas cDNA library and sequenced. This cDNA (1620 bp) includes an entire open reading frame encoding mature protein (128 aa) following a signal peptide (28 aa) as well as 5'- and 3'-untranslated regions.
M, Seno +4 more
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Pancreatic Ribonuclease Distribution and Comparisons in Mammals
Nature New Biology, 1973PANCREATIC RNAase is absent or present in very small amounts in the pancreas of species such as man, cat, seal and rabbit1. Likewise no RNAase activity has been found in the pancreatic juice of dog by Marchis-Mouren et al.2 and in the juice of cat and rabbit by Berndt3.
BEINTEMA, JJ +4 more
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1982
Publisher Summary Bovine Ribonuclease has been a test protein in the study of a wide variety of chemical and physical methods of protein chemistry. It is widely employed in the course of the sequencing of RNA. This chapter discusses the usefulness of the cytoplasmic inhibitor of RNase to protect RNA in the course of the synthesis of complementary DNA
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Publisher Summary Bovine Ribonuclease has been a test protein in the study of a wide variety of chemical and physical methods of protein chemistry. It is widely employed in the course of the sequencing of RNA. This chapter discusses the usefulness of the cytoplasmic inhibitor of RNase to protect RNA in the course of the synthesis of complementary DNA
openaire +1 more source