scholarly journals The green hemoproteins of bovine erythrocytes. I purification and characterization.

1978 ◽  
Vol 253 (9) ◽  
pp. 2946-2953
Author(s):  
L.J. DeFilippi ◽  
D.E. Hultquist
Keyword(s):  
Purification And Characterization ◽  
Bovine Erythrocytes

Purification and characterization of two forms of Cu/Zn-superoxide dismutase from bovine erythrocytes by preparative isoelectric focusing

1981 ◽  
Vol 46 (9) ◽  
pp. 2140-2145 ◽  
Author(s):  
Hana Kovářová ◽  
Jan Šimša ◽  
Josef Křížala
Keyword(s):  
Superoxide Dismutase ◽  
Isoelectric Focusing ◽  
Visible Region ◽  
Alkaline Media ◽  
Ultraviolet Region ◽  
Purification And Characterization ◽  
Isoelectric Points ◽  
Relative Molecular Weight ◽  
Bovine Erythrocytes

Two forms of Cu/Zn-superoxide dismutase with isoelectric points (pI) 6.3 and 5.2 were isolated from bovine erythrocytes by preparative isoelectric focusing. Both forms show a relative molecular weight of 32 000 daltons corresponding to the value reported for the monomer molecule. From spectral analysis the maximum in the ultraviolet region of the spectrum (276 nm) is identical for both forms of superoxide dismutase whereas the maxima in the visible region are different (for the pI 5.2 form the maximum lies at 405 nm and for the pI 6.3 form at 695 nm). The different migration of the enzymatically active zones toward the anode during electrophoresis in alkaline media corresponds to their different isoelectric points.

Hemolysis of erythrocytes by the hemolytic system from the blood-feeding stable fly, Stomoxys calcitrans

1992 ◽  
Vol 50 (1) ◽  
pp. 690-691
Author(s):  
H. J. Kirch ◽  
G. Spates ◽  
R. Droleskey ◽  
W.J. Kloft ◽  
J.R. DeLoach
Keyword(s):  
Blood Feeding ◽  
Stomoxys Calcitrans ◽  
Stable Fly ◽  
Digestive Physiology ◽  
Transmission Electron ◽  
Erythrocyte Lysis ◽  
Mammalian Blood ◽  
Bovine Erythrocytes ◽  
Potential Tool

Blood feeding insects have to rely on the protein content of mammalian blood to insure reproduction. A substantial quantity of protein is provided by hemoglobin present in erythrocytes. Access to hemoglobin is accomplished only via erythrocyte lysis. It has been shown that midgut homogenates from the blood feeding stable fly, Stomoxys calcitrans, contain free fatty acids and it was proposed that these detergent-like compounds play a major role as hemolysins in the digestive physiology of this species. More recently sphingomyelinase activity was detected in midgut preparations of this fly, which would provide a potential tool for the enzymatic cleavage of the erythrocyte's membrane sphingomyelin. The action of specific hemolytic factors should affect the erythrocyte's morphology. The shape of bovine erythrocytes undergoing in vitro hemolysis by crude midgut homogenates from the stable fly was examined by scanning and transmission electron microscopy.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Sign in / Sign up

Export Citation Format

Share Document