Hemoglobin peroxidase reaction of hemoglobin efficiently catalyzes oxidation of benzo[a]pyrene

Chemosphere ◽  
2020 ◽  
pp. 128795
Author(s):  
Haein Keum ◽  
Juhee Kim ◽  
Yong Hoon Joo ◽  
Guyoung Kang ◽  
Namhyun Chung
Keyword(s):  
Peroxidase Reaction

Three-Dimensional Visualization of the T-System of Frog Muscle Using High Voltage Electron Microscopy and a Lanthanum Stain

1977 ◽  
Vol 35 ◽  
pp. 570-571 ◽  
Author(s):  
Lee D. Peachey ◽  
Clara Franzini-Armstrong
Keyword(s):  
Electron Microscopy ◽  
High Voltage ◽  
Three Dimensional ◽  
Biological Tissues ◽  
High Voltage Electron Microscopy ◽  
Transverse Tubular System ◽  
Peroxidase Reaction ◽  
Voltage Electron ◽  
High Voltage Electron ◽  
T System

The effective study of biological tissues in thick slices of embedded material by high voltage electron microscopy (HVEM) requires highly selective staining of those structures to be visualized so that they are not hidden or obscured by other structures in the image. A tilt pair of micrographs with subsequent stereoscopic viewing can be an important aid in three-dimensional visualization of these images, once an appropriate stain has been found. The peroxidase reaction has been used for this purpose in visualizing the T-system (transverse tubular system) of frog skeletal muscle by HVEM (1). We have found infiltration with lanthanum hydroxide to be particularly useful for three-dimensional visualization of certain aspects of the structure of the T- system in skeletal muscles of the frog. Specifically, lanthanum more completely fills the lumen of the tubules and is denser than the peroxidase reaction product.

scholarly journals Abnormal or Pathological Leucocytes, as They Appear under the Copper Peroxidase Reaction

1936 ◽  
Vol 28 (4-5) ◽  
pp. 285-288
Author(s):  
Akira Sato ◽  
Tamotsu Suzuki ◽  
Ryoji Shibata
Keyword(s):  
Peroxidase Reaction

scholarly journals Cetyltrimethylammonium Ion Stabilization of Tribromide Ion from Peroxidase Reaction.

1987 ◽  
Vol 41b ◽  
pp. 422-425 ◽  
Author(s):  
Lars G. Öberg ◽  
Ann-Marie Eklund ◽  
Curt R. Enzell ◽  
Jan-Eric Berg ◽  
Lennart Eberson
Keyword(s):  
Peroxidase Reaction

Peroxidase Reaction as a Parameter for Discrimination of Streptococcus mutans and Streptococcus sobrinus

2001 ◽  
Vol 35 (4) ◽  
pp. 258-264 ◽  
Author(s):  
S. Rupf ◽  
K. Merte ◽  
K. Eschrich ◽  
L. Stösser ◽  
S. Kneist
Keyword(s):  
Streptococcus Mutans ◽  
Streptococcus Sobrinus ◽  
Peroxidase Reaction

CHAOS IN BIOCHEMICAL SYSTEMS: THE PEROXIDASE REACTION AS A CASE STUDY

1993 ◽  
pp. 175-224 ◽  
Author(s):  
RAIMA LARTER ◽  
LARS FOLKE OLSEN ◽  
CURTIS G. STEINMETZ ◽  
TORBEN GEEST
Keyword(s):  
Peroxidase Reaction ◽  
Biochemical Systems

Continuous-flow fluorometry of low galactose concentrations in blood or plasma.

1980 ◽  
Vol 26 (2) ◽  
pp. 282-285 ◽  
Author(s):  
J M Henderson ◽  
F W Fales
Keyword(s):  
Blood Flow ◽  
Hepatic Blood Flow ◽  
Continuous Flow ◽  
Normal Subjects ◽  
Galactose Oxidase ◽  
Fluorogenic Substrate ◽  
Flow Method ◽  
Peroxidase Reaction ◽  
Hydroxyphenylacetic Acid ◽  
Continuous Flow Method

Abstract Clearance of 0-100 mg/L concentrations of galactose from the blood depends on nutrient hepatic blood flow. We can measure such concentrations, which was not previously possible, by a continuous-flow method involving the use of galactose oxidase and peroxidase, the latter being coupled to a fluorogenic substrate, p-hydroxyphenylacetic acid. Interfering substances in the peroxidase reaction are removed by zinc/alkali precipitation. Sensitivity is maximized by using saturating concentrations of the enzymes and substrate. In prepared plasma test samples with galactose concentrations of 10, 40, 70, and 100 mg/L, the within-run CV's ranged from 2.1 to 8.6%, and day-to-day CV's from 2.2 to 17.2%, the largest CV's being for the 10 mg/L concentration. Normal subjects are shown to clear galactose more efficiently than subjects with moderate cirrhosis.

scholarly journals Normal Leucocytes, as They Appear under the Copper Peroxidase Reaction

1934 ◽  
Vol 24 (3) ◽  
pp. 195-201
Author(s):  
Akira Sato ◽  
Tamotsu Suzuki ◽  
Ryoji Shibata
Keyword(s):  
Peroxidase Reaction
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