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Bovine pancreas ribonuclease

Protein adsorption on solid surfaces is discussed from a colloid chemical and thermodynamic point of view. Information is mainly obtained from adsorption isotherms, (proton)titrations, electrokinetics and calorimetry. The adsorption behavior of human plasma albumin and bovine pancreas ribonuclease at various surfaces is studied. The differences in behavior between the two proteins are related to differences in the structural properties. Furthermore, the essential role of the low molecular weight electrolytes in the overall protein adsorption process is stressed. [Pg.36]

Figure 2. Plateau values for the adsorption of bovine pancreas ribonuclease on polystyrene latex (o), polyoxymethylene ( ) and hematite (x). Conditions as in Figure 1. Figure 2. Plateau values for the adsorption of bovine pancreas ribonuclease on polystyrene latex (o), polyoxymethylene ( ) and hematite (x). Conditions as in Figure 1.
Figure A. Charge transfer (expressed per unit area of the sorbent surface) between the solution and adsorbed layers of human plasma albumin (HPA) and bovine pancreas ribonuclease (RNase) on various sorbents. Plateau adsorption. Figure A. Charge transfer (expressed per unit area of the sorbent surface) between the solution and adsorbed layers of human plasma albumin (HPA) and bovine pancreas ribonuclease (RNase) on various sorbents. Plateau adsorption.
Figure 4.8 Cation-exchange liquid chromatography of basic proteins. Column, Asahipak ES502C eluent, 20 min linear gradient of sodium chloride from 0 to 500 mM in 50 mM sodium phosphate buffer pH 7.0 flow rate, 1 ml min-1 temperature, 30 °C detection, UV 280 nm. Peaks 1, myoglobin from horse skeletal muscle (Mr 17 500, pi 6.8-7.3) 2, ribonuclease from bovine pancreas (Mr 13 700, pi 9.5-9.6) 3, a-chymotrypsinogen A from bovine pancreas (Mr 257 000, pi 9.5) and 4, lysozyme from egg white (Mr 14 300, pi 11.0-11.4). (Reproduced by permission from Asahikasei data)... Figure 4.8 Cation-exchange liquid chromatography of basic proteins. Column, Asahipak ES502C eluent, 20 min linear gradient of sodium chloride from 0 to 500 mM in 50 mM sodium phosphate buffer pH 7.0 flow rate, 1 ml min-1 temperature, 30 °C detection, UV 280 nm. Peaks 1, myoglobin from horse skeletal muscle (Mr 17 500, pi 6.8-7.3) 2, ribonuclease from bovine pancreas (Mr 13 700, pi 9.5-9.6) 3, a-chymotrypsinogen A from bovine pancreas (Mr 257 000, pi 9.5) and 4, lysozyme from egg white (Mr 14 300, pi 11.0-11.4). (Reproduced by permission from Asahikasei data)...
Ribonuclease A, Bovine pancreas. Horse heart. AOT/isooctane Solubilization [72]... [Pg.131]

In view of the high stability of the enzyme most samples have been prepared by the procedure described by Kunitz (16) and modified by McDonald (17) to remove all traces of proteolytic activity. During this procedure the minced bovine pancreas is exposed to 0.25 N sulfuric acid, ammonium sulfate precipitation, 10 min at 95°-100° and pH 3, and, finally, reprecipitation. The product can be crystallized it was also shown later to contain a number of components all with ribonuclease activity. A practical summary of all details is given by Kunitz and McDonald (18). [Pg.649]

MATERIALS. Ribonuclease A (RNase A) (bovine pancreas), cytochrome C (Cyt. C) (horse heart), lysozyme (chicken egg white), myoglobin (sperm whale), P-lactoglobulin A... [Pg.166]

Ribonuclease I Bovine pancreas RNA endonuclease splits d bonds where pyrimidine nucleotides are in 3 position... [Pg.285]

Many of the nucleic acid hydrolases occur in isoenzymic forms in mammalian tissues. Some of these isoenzymes are glycoenzymes, and information on these is contained in Table I. Ribonuclease B has been studied in the greatest detail. Following the initial observation that the ribonuclease from bovine pancreas occurs in isoenzymic forms,45 it was found that one form (ribonuclease B) contains an appreciable... [Pg.307]

Ribonuclease, immobilized on EupergitC Origin bovine pancreas... [Pg.1497]

Having considered some of the mechanisms of hydrolysis, it is of interest to compare these with the active site mechanism of a few enzymes which catalyze such reactions. The enzyme ribonuclease A (RNase A) (bovine pancreas, MW = 13,680, one polypeptide chain consisting of 124 amino acid residues) catalyzes the degradation of RNA by a two-step mechanism transesterification followed by hydrolysis of the five-membered cyclic inter-... [Pg.115]


See other pages where Bovine pancreas ribonuclease is mentioned: [Pg.122]    [Pg.123]    [Pg.5]    [Pg.1776]    [Pg.38]    [Pg.148]    [Pg.234]    [Pg.235]    [Pg.284]    [Pg.122]    [Pg.123]    [Pg.5]    [Pg.1776]    [Pg.38]    [Pg.148]    [Pg.234]    [Pg.235]    [Pg.284]    [Pg.86]    [Pg.112]    [Pg.509]    [Pg.155]    [Pg.509]    [Pg.87]    [Pg.446]    [Pg.446]    [Pg.648]    [Pg.373]    [Pg.306]    [Pg.308]    [Pg.141]    [Pg.181]    [Pg.476]    [Pg.1497]    [Pg.174]    [Pg.87]    [Pg.302]    [Pg.452]    [Pg.562]    [Pg.9]    [Pg.4511]    [Pg.607]    [Pg.16]    [Pg.249]    [Pg.372]    [Pg.194]    [Pg.170]    [Pg.111]   
See also in sourсe #XX -- [ Pg.388 ]




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