2 edition of purification and characterization of a ribonuclease from bovine aorta found in the catalog.
purification and characterization of a ribonuclease from bovine aorta
Roger Allen Lewis
Written in English
|Statement||by Roger Allen Lewis.|
|The Physical Object|
|Pagination||80 leaves, bound :|
|Number of Pages||80|
Bovine retinas contain a factor that stimulates proliferation of aortic endothelial cells in culture as well as neovascularization on the chicken chorioallantoic membrane. The stimulatory activity has been partially purified from a balanced salt solution extract of bovine by: Abstract. Apyrases or ATP diphosphohydrolases (ATPDases: EC ) first mentioned by Meyerhof in 1 refer to a family of enzymes that catalyse the hydrolysis of the γ and β phosphate residues of triphospho- and diphosphonucleosides. The original report by Kalckar in 2 of an ATPDase in potato extracts initiated a series of studies on this enzyme (for reviews see 3, 4).Cited by: 9.
Source: Bovine Pancreas I.U.B.: Pancreatic ribonuclease (RNase I) catalyzes cleavage of the phosphodiester bond between the 5'-ribose of a nucleotide and the phosphate group attached to the 3'-ribose of an adjacent pyrimidine nucleotide forming a 2',3'-cyclic phosphate which may then be hydrolyzed to the corresponding 3'-nucleoside phosphate. Ribonuclease A from bovine pancreas for molecular biology, ≥70 Kunitz units/mg protein, lyophilized.
Ribonuclease A from bovine pancreas Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein. Purification and characterization of a ribonuclease from human liver. S Sorrentino, G K Tucker and The major ribonuclease of human liver has been isolated in a four-step procedure. The protein appears homogeneous by several criteria. The amino acid composition and the amino-terminal sequence of the enzyme indicate that the protein is.
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Aorta ribonuclease I appeared to be homogeneous when subjected to discontinuous gel electrophoresis. Aorta ribonuclease II exhibited the same properties as aorta ribonuclease previously isolated.
The activities of the aorta ribonucleases and pancreatic ribonuclease on homopolymers and dinucleoside phosphates were compared. by: 3. Purification and characterization of bovine aorta ribonucleases. Lewis R GAMBLE W. Two ribonucleases (aorta ribonuclease I and aorta ribonuclease II) from bovine aorta were purified fold and fold by: 3.
The present study is concerned with the purification and characterization of an aortic ribonuclease. An endonuclease (ARNase I) isolated from the bovine aorta has been purified fold by means of fractionation with ethanol, acid extraction, isoionic precipitation, BioRex 70 column chromatography and : Roger Allen Lewis.
Purification and Characterization of a Ribonuclease from Human Liver* (Received for publication, April 8, ) Salvatore SorrentinoS, Gabrielle Kapor Tucker, and Dohn G. Glitz From the DeDartment of Bioloeical Chemistrv.
UCLA School of Medicine, University of. P6ytocliemistry, No 7, ppPrinted in Great Britain /85 $+0 00 Pergamon Press Ltd PURIFICATION AND CHARACTERIZATION OF A RIBONUCLEASE FROM BARLEY ROOTS* N. PRENTICE and S. HEISELt U S. Department of Agriculture, Agricultural Research Service, Cereal Crops Research Unit, N.
Walnut Street, Madison, WIU.S.A. (Received 21 Cited by: 9. The present study is concerned with the purification\ud and characterization of an aortic ribonuclease.\ud An endonuclease (ARNase I) isolated from the bovine aorta has\ud been purified fold by means of fractionation with ethanol, acid\ud extraction, isoionic precipitation, BioRex 70 column chromatography\ud and dialysis.
Bovine skeletal muscle contains small amounts of at least six heat- and acid-stable RNA-degrading enzymes. Our results are the first evidence for multiple ribonucleases in skeletal muscle. Three of these have been highly purified, and each has been shown to be a pyrimidine-specific endoribonuclease by use of a rapid sequencing technique employing gel by: 4.
European journal of biochemistry Purification and characterization of a novel protein from bovine aorta that inhibits coagulation. Inhibition of the phospholipid-dependent factor-Xa-catalyzed prothrombin activation, through a high-affinity binding of the anticoagulant to the phospholipids.
It would appear, therefore, that some bovine ribonucleases differ from bovine pancreatic ribonuclease. The present report describes the isolation and partial purification of a ribonuclease from bovine aorta.
The bovine aorta ribonuclease seems to be free of deoxyribonuclease, phosphomonoesterase, and cyclic phosphatase by: 3. Bovine pancreatic ribonuclease is the most characterized of all nucleases and was the first enzyme to be subjected to sequencing, protein crystallographic, and protein folding studies.
Currently there are hundreds of known RNases that have been fully or partially characterized, with many more to be by: 3. Purification from normal human plasma and biochemical characterization of a ribonuclease specific for poly(C) and poly(U). Archives of Biochemistry and Biophysics(1), DOI: /S(03) Deepak Gaur, Divya Seth, Janendra K by: Purification and characterization of bovine aorta ribonucleases.
By R. Lewis and W. Gamble. Abstract. Two ribonucleases (aorta ribonuclease I and aorta ribonuclease II) from bovine aorta were purified fold and fold respectively.
Ethanolic precipitation, acid extraction, isoionic precipitation at pH35 and Bio-Rex 70 column Author: R. Lewis and W. Gamble. Purification of RNase from Bacillus sp. RNS3. The bacterial RNase was purified by ammonium sulphate precipitation followed by gel permeation chromatography using Sephadex G All the purification steps were carried out at 4 °C unless stated otherwise.
Step 1: Removal of biomass and ammonium sulphate precipitationCited by: 1. Purification and characterization of a new ribonuclease from fruiting bodies of the oyster mushroom Pleurotus ostreatus. The N‐terminal sequence of Pleurotus ostreatus RNase did not manifest homology even to a previously reported RNase from the same mushroom.
The ribonuclease was adsorbed on CM‐Sepharose and Mono by: A purification procedure for the isolation of homogeneous preparations of bovine aorta amine oxidase and a study of its lysyl oxidase activity. Biochimica et Biophysica Acta (BBA) - Enzymology(2), DOI: /(75)Cited by: Purified bovine liver ribonuclease, as well as rat and porcine liver-type ribonucleases were used for studies of enzyme specificity.
Table 1 presents enzymic activities of bovine ribonuclease A and these three liver-type ribonucleases on poly(C) and poly(U). The liver-type ribonucleases are less active on both substrates than bovine ribonuclease by: Ribonuclease A (RNase A) is an endoribonuclease that attacks at the 3 phosphate of a pyrimidine nucleotide.
The sequence of pG-pG-pC-pA-pG will be cleaved to give pG-pG-pCp and A-pG. The highest activity is exhibited with single-stranded RNA.1 RNase A is a single chain polypeptide containing 4 disulfide bridges. In contrast to RNase B, RNase A is.
An RNase with a molecular mass of 28 kDa and with high ribonucleolytic activity toward poly(A) was purified from the ascocarps of Tuber purification procedure involved ion exchange chromatography on diethylaminoethyl cellulose, Q‐Sepharose and Mono Q, and gel filtration by fast protein liquid chromatography on Superdex Cited by: 6.
Characterization of the Tryptophan Residues of Human Placental Ribonuclease Inhibitor and Its Complex with Bovine Pancreatic Ribonuclease A by Steady-State and Time-Resolved Emission Spectroscopy. The Journal of Physical Chemistry B(42), ANALYTICAL BIOCHEMISTRY() Ribonuclease Inhibitor from Pig Brain: Purification, Characterization, and Direct Spectrophotometric Assay' Sungwoo Cho and J.
Joshi2 Department of Biochemistry, The University of Tennessee, Knoxuille, Tennessee Received Ap The ribonuclease inhibitor from pig brain has been purified fold by a combination Cited by:. Purification and characterization of a ribonuclease with antiproliferative activity from the mystical wild mushroom Tuber indicum.
Chen Xiao. State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, China Cited by: 6. T1 - Expression, purification, and characterization of a recombinant ribonuclease H from Thermus thermophilus HB8.
AU - Kanaya, S. AU - Itaya, M. PY - /7/ Y1 - /7/ N2 - Thermus thermophilus ribonuclease H was overexpressed and purified from Escherichia by: Title: THE PURIFICATION AND CHARACTERIZATION OF A RIBONUCLEASE FROM BOVINE AORTA Abstract approved: Redacted for privacy Wilbert Gamble Reports of investigations on nucleases in arterial tissue are few in number.
The present study is concerned with the purifica- tion and characterization of an aortic ribonuclease.