Purification of ribulose-1,5-bisphosphate carboxylase/oxygenase with high specific activity by fast protein liquid chromatography

1986 ◽  
Vol 153 (1) ◽  
pp. 97-101 ◽  
Author(s):  
Michael E. Salvucci ◽  
Archie R. Portis ◽  
William L. Ogren
Keyword(s):  
Liquid Chromatography ◽  
Specific Activity ◽  
High Specific Activity ◽  
Fast Protein Liquid Chromatography ◽  
Bisphosphate Carboxylase

High specific activity ribulose 1,5-bisphosphate carboxylase-oxygenase from Nicotiana tabacum

1981 ◽  
Vol 2 (4) ◽  
pp. 235-242 ◽  
Author(s):  
James T. Bahr ◽  
Sarjit Johal ◽  
Malcolm Capel ◽  
Don P. Bourque
Keyword(s):  
Nicotiana Tabacum ◽  
Specific Activity ◽  
High Specific Activity ◽  
Bisphosphate Carboxylase

scholarly journals Partial purification of goat kidney β-mannosidase

1988 ◽  
Vol 249 (3) ◽  
pp. 871-875 ◽  
Author(s):  
J I Frei ◽  
K T Cavanagh ◽  
R A Fisher ◽  
R P Hausinger ◽  
M Dupuis ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Cation Exchange ◽  
Anion Exchange ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Fast Protein Liquid Chromatography ◽  
Partial Purification

1. Goat kidney beta-mannosidase was purified 8500-fold to a specific activity of 65,000 nmol/h per mg of protein with a 6% yield by using multiple steps including cation-exchange and anion-exchange fast protein liquid chromatography. This is the first description of a highly purified preparation from goat tissue; however, it was not homogeneous, as judged by silver-stained SDS/polyacrylamide-gel electrophoresis. 2. The enzyme exhibited microheterogeneity when analysed by isoelectric focusing (pI 5.5-6.5). 3. Purified beta-mannosidase hydrolysed the terminal beta-(1→4)-linkage of oligosaccharides that accumulate in beta-mannosidosis.

scholarly journals The autotrophic growth of Micrococcus denitrificans on Methanol

1975 ◽  
Vol 150 (3) ◽  
pp. 569-571 ◽  
Author(s):  
R B Cox ◽  
J R Quayle
Keyword(s):  
Specific Activity ◽  
Carbon Assimilation ◽  
High Specific Activity ◽  
Ribulose Bisphosphate Carboxylase ◽  
Autotrophic Growth ◽  
Ribulose Bisphosphate ◽  
Bisphosphate Carboxylase ◽  
Physiological Evidence

Ribulose bisphosphate carboxylase is present at a high specific activity in extracts of methanol-grown Microccus denitrificans. Enzymic and physiological evidence indicates that, during growth on methanol, the ribulose bisphosphate cycle is the route of carbon assimilation.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

Autoprothrombin C Activity from Prothrombin with Snake Venom or Trypsin

1962 ◽  
Vol 08 (03) ◽  
pp. 425-433 ◽  
Author(s):  
Ewa Marciniak ◽  
Edmond R Cole ◽  
Walter H Seegers
Keyword(s):  
Snake Venom ◽  
Thrombolytic Agent ◽  
Sodium Citrate ◽  
Specific Activity ◽  
High Specific Activity ◽  
Citrate Solution ◽  
Clotting Factors ◽  
Activation Products ◽  
Russell’S Viper ◽  
Autoprothrombin C

SummarySuitable conditions were found for the generation of autoprothrombin C from purified prothrombin with the use of Russell’s viper venom or trypsin. DEAE chromatographed prothrombin is structurally altered and has never been found to yield autoprothrombin C and also did not yield it when Russell’s viper venom or trypsin were used. Autoprothrombin C is derived from prothrombin with tissue extract thromboplastin, but not in large amounts with the intrinsic clotting factors. With the latter thrombin and autoprothrombin III are the chief activation products. Autoprothrombin III concentrates were prepared from serum and upon activation with 25% sodium citrate solution or with Russell’s viper venom large amounts of autoprothrombin C were obtained, and this was of high specific activity. Theoretically trypsin is not a thrombolytic agent, but on the contrary should lead to intravascular clotting.

Synthesis and properties of [2-[3,5-3H2]-tyrosine,4-glutamic acid]deamino-1-carba-oxytocin

1984 ◽  
Vol 49 (8) ◽  
pp. 1921-1926 ◽  
Author(s):  
Michal Lebl ◽  
Tomislav Barth ◽  
Denis J. Crankshaw ◽  
Bohuslav Černý ◽  
Edwin E. Daniel ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Glutamic Acid ◽  
Title Compound ◽  
Specific Activity ◽  
Reversed Phase ◽  
Reversed Phase Liquid Chromatography ◽  
Phase Liquid

The title compound (specific activity 11.1-32.7 Ci (0.41-1.22 TBq)/mmol) was prepared by iodination and subsequent catalytic replacement of iodine by tritium. The analogue which was unstable in the form of a lyophilizate was purified by reversed phase liquid chromatography. Using the N,N'-dicyclohexylcarbodiimide method, the pure analogue was converted into N-hydroxybenzotriazolyl ester, an irreversible oxytocin inhibitor. However, attempts to label specifically the uterotonic receptor, present in the enriched rat myometrium fraction, were hithero unsuccessful

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