scholarly journals Glycerol Impact on Human and Bovine Erythrocytes Under Hypertonic Shock

2019 ◽  
Vol 29 (3) ◽  
pp. 199-205
Author(s):  
Olena Nipot ◽  
◽  
Natalya Yershova ◽  
Olga Shapkina ◽  
Sergiy Yershov ◽  
...  
Keyword(s):  
Hypertonic Shock ◽  
Bovine Erythrocytes

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.

Comparative study of sensitivity of bovine and ram erythrocytes to post-hypertonic shock

2017 ◽  
Vol 19 (2) ◽  
pp. 64-69
Author(s):  
A. A. Mazur ◽  
◽  
E. Ye. Nipot ◽  
N. V. Orlova ◽  
N. M. Shpakova ◽  
...  
Keyword(s):  
Comparative Study ◽  
Hypertonic Shock

Babesia bovis: Purification and concentration of merozoites and infected bovine erythrocytes

1986 ◽  
Vol 61 (2) ◽  
pp. 236-243 ◽  
Author(s):  
S.D. Rodriguez ◽  
G.M. Buening ◽  
C.A. Vega ◽  
C.A. Carson
Keyword(s):  
Babesia Bovis ◽  
Bovine Erythrocytes

scholarly journals Differences in the permeability of bovine erythrocytes to fructose

1971 ◽  
Vol 122 (5) ◽  
pp. 55P.1 ◽  
Author(s):  
I A Nimmo ◽  
J G Hall
Keyword(s):  
Bovine Erythrocytes

scholarly journals Acetylcholinesterase aus Rindererythrozyten. Reinigung und Eigenschaften des mit und ohne Triton X-100 solubilisierten Enzyms / Acetylcholinesterase from Bovine Erythrocytes. Purification and Properties of the En­zyme Solubilized in the Presence and the Absence of Triton X-100

1979 ◽  
Vol 34 (9-10) ◽  
pp. 721-725 ◽  
Author(s):  
Heinz Großmann ◽  
Manfred Liefländer
Keyword(s):  
Amino Acid ◽  
Specific Activity ◽  
Multiple Forms ◽  
Terminal Amino Acid ◽  
Enzyme Preparations ◽  
Purification And Properties ◽  
Solubilized Enzyme ◽  
Terminal Amino ◽  
Triton X ◽  
Bovine Erythrocytes

Abstract Acetylcholinesterase was released from bovine erythrocytes by Triton X-100 treatment and pu­rified by twofold affinity chromatography. The detergentfree enzyme was obtained with a specific activity of 4130 U /mg (303 000-fold purification) and a 25% yield. Alternatively, the commercial available crude enzyme was purified. The latter preparation has an uniform molecular weight (Mr 175 000). The Triton-solubilized enzyme, however, can be resolved after removal of the detergent in eight multiple forms (Mr 175 000 and multiple values), in the presence of Triton there exists only one form (Mr 338 000). The amino acid composition of the two enzyme preparations differs significantly. No differences were observed with respect to other properties: SDS gel electrophore­sis revealed two protein bands (Mr 166 000 and 86 000) with both preparations. The enzyme is a glycoprotein with a pI value of 4.3 and contains strongly bound phosphatidylethanolamine. The N-terminal amino acid has been found to be Glu (or Gin).

scholarly journals Bacteriorhodopsin induces a light-scattering change in Halobacterium halobium.

1978 ◽  
Vol 79 (3) ◽  
pp. 657-662 ◽  
Author(s):  
C L Wey ◽  
P L Ahl ◽  
R A Cone
Keyword(s):  
Absorption Spectrum ◽  
Light Scattering ◽  
Near Infrared ◽  
Action Spectrum ◽  
Bright Light ◽  
Infrared Region ◽  
Halobacterium Halobium ◽  
Scattering Response ◽  
Near Infrared Region ◽  
Hypertonic Shock

When suspensions of Halobacterium halobium are exposed to bright light, the light-scattering properties of the bacteria change. This light-scattering response can produce a transmission decrease of about 1% throughout the red and near-infrared region. The action spectrum for the light-scattering response appropriately matches the absorption spectrum of bacteriorhodopsin. The response is eliminated by cyanide p-trifluoro-methoxyphenylhydrazone, a proton ionophore, and by triphenylmethylphosphonium, a membrane permanent cation. A mild hypertonic shock induces a similar light-scattering change, suggesting that bright light causes the bacteria to shrink about 1% in volume, thereby producing the light-scattering response.

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