The histochemical demonstration of aniline hydroxylase activity in rat liver

1971 ◽  
Vol 3 (2) ◽  
pp. 107-116 ◽  
Author(s):  
S. Gangolli ◽  
M. Wright
Keyword(s):  
Rat Liver ◽  
Histochemical Demonstration ◽  
Hydroxylase Activity ◽  
Aniline Hydroxylase

Modulation of Microsomal Cytochrome P450 by Scutellariae Radix and Gentianae Scabrae Radix in Rat Liver

1996 ◽  
Vol 24 (01) ◽  
pp. 19-29 ◽  
Author(s):  
Jaw-Jou Kang ◽  
Yi-Chien Chen ◽  
Wei-Chung Kuo ◽  
Terri Chen ◽  
Yu-Wen Cheng ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Medicinal Herbs ◽  
Hydroxylase Activity ◽  
Microsomal Cytochrome ◽  
Aniline Hydroxylase ◽  
Scutellariae Radix ◽  
Microsomal Cytochrome P450 ◽  
Pyrene Hydroxylase

The present study has determined the effects of Scutellariae Radix (Huangqin) and Gentianae scabrae Radix (Longdan) on liver microsomal cytochrome P450 (P450)-dependent mono-oxygenases using rats pretreated with crude extracts of medicinal herbs. Scutellariae Radix resulted in a 53% decrease of pentoxyresorufin O-dealkylase activity in liver microsomes. In contrast, Gentianae scabrae Radix caused a 50% increase of benzo(a)pyrene hydroxylase activity. Immunoblotting 1A and 2B proteins, respectively. Scutellariae and Gentianae scabrae Radixes had no effects on microsomal aniline hydroxylase activity and P450 2E1 protein.

Development of vitamin D3 25-hydroxylase activity in rat liver microsomes

1986 ◽  
Vol 250 (1) ◽  
pp. 120-127 ◽  
Author(s):  
Myrtle Thierry-Palmer ◽  
Suzanne Cullins ◽  
Shakoora Rashada ◽  
T.Kenney Gray ◽  
Almena Free
Keyword(s):  
Rat Liver ◽  
Vitamin D3 ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Hydroxylase Activity

Histochemical demonstration of enzymes in rat liver during post-natal development

1970 ◽  
Vol 23 (1) ◽  
pp. 71-81 ◽  
Author(s):  
J. Koudstaal ◽  
M. J. Hardonk
Keyword(s):  
Rat Liver ◽  
Histochemical Demonstration

Comparison of Different Methods for the Determination of Phenylalanine Hydroxylase Activity in Rat Liver and Euglena gracilis

1984 ◽  
Vol 39 (7-8) ◽  
pp. 728-733 ◽  
Author(s):  
Rita M. Fink ◽  
Erich F. Elstner
Keyword(s):  
Rat Liver ◽  
Euglena Gracilis ◽  
Phenylalanine Hydroxylase ◽  
Hplc Method ◽  
Enzymic Activity ◽  
Hydroxylase Activity ◽  
Product Separation ◽  
Tyrosine Concentration ◽  
Layer Chromatography

Abstract Three different methods for the determination of phenylalanine hydroxylase activity have been compared: a) Differential photometric assay of the increase in tyrosine concentration in the presence of phenylalanine; b) Product separation by thin layer chromatography and scintillation counting of the [14C]tyrosine formed;c) HPLC separation and spectrofluorometric quantification of derivatized amino acids. A comparison of the activities of phenylalanine hydroxylase in rat liver and Euglena gracilis clearly showed that only rat liver contains this enzymic activity as shown by methods b) and c) although pseudo-activity of Euglena gracilis preparations was found during the spectrophotometric test a). The HPLC method proved to be the fastest, most reliable and convenient method for direct tyrosine determination and thus for measuring phenylalanine hydroxylase activity.

Evaluation of Lesion Scoring and Aniline Hydroxylase Activity in Hepatocarcinogenesis Rats Treated with Strobilanthes crispus

2004 ◽  
Vol 5 (1) ◽  
pp. 26-30 ◽  
Author(s):  
O. Fauziah ◽  
P. Hanachi ◽  
S. Yogespiriy ◽  
R. Asmah
Keyword(s):  
Hydroxylase Activity ◽  
Aniline Hydroxylase ◽  
Strobilanthes Crispus

The Interaction of the Antineoplastic Drug Thalicarpine with Aniline Hydroxylase and Microsomal Cytochrome of Rat Liver

Xenobiotica ◽  
1974 ◽  
Vol 4 (4) ◽  
pp. 255-261 ◽  
Author(s):  
Patrick J. Creaven ◽  
Larry M. Allen ◽  
Carole P. Williams
Keyword(s):  
Rat Liver ◽  
Antineoplastic Drug ◽  
Microsomal Cytochrome ◽  
Aniline Hydroxylase

Inhibition of rat liver calciferol 25-hydroxylase activity with anticonvulsant drugs

Life Sciences ◽  
1977 ◽  
Vol 21 (9) ◽  
pp. 1317-1322 ◽  
Author(s):  
S. Sulimovici ◽  
M.S. Roginsky
Keyword(s):  
Rat Liver ◽  
Anticonvulsant Drugs ◽  
Hydroxylase Activity

scholarly journals Intracellular enzymes of collagen biosynthesis in rat liver as a function of age and in hepatic injury induced by dimethylnitrosamine. Purification of rat prolyl hydroxylase and comparison of changes in prolyl hydroxylase activity with changes in immunoreactive prolyl hydroxylase

1976 ◽  
Vol 158 (2) ◽  
pp. 369-376 ◽  
Author(s):  
J Risteli ◽  
L Tuderman ◽  
K I Kivirikko
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Hepatic Injury ◽  
Specific Activity ◽  
Prolyl Hydroxylase ◽  
Newborn Rats ◽  
Hydroxylase Activity ◽  
Immunoreactive Protein ◽  
Molecular Weights ◽  
Polypeptide Chains

Prolyl hydroxylase was purified from newborn rats by affinity chromatography using poly(L-proline), and antiserum to the enzyme was prepared in rabbits. The rat prolyl hydroxylase was similar to the chick and human enzymes with respect to specific activity, molecular weight and molecular weights of the polypeptide chains. The activity of prolyl hydroxylase and the content of immunoreactive enzyme were measured in rat liver as a function of age in experimental hepatic injury. Active prolyl hydroxylase comprised about 13.2% of the total immunoreactive protein in the liver of newborn rats and the value decreased to about 3.6% at the age of 420 days. This decrease was due to a decrease in the enzyme activity, whereas only minor changes were found in the content of the immunoreactive protein. In hepatic injury, a significant increase was found in the ratio of active enzyme to total immunoreactive protein, owing to an increase in the enzyme activity. The data indicate that prolyl hydroxylase activity in rat liver is controlled in part by a mechanism which does not involve changes in the content of the total immunoreactive protein.

scholarly journals Freeze substituted tissue in 5'-nucleotidase histochemistry. Comparative histochemical and biochemical investigations.

1979 ◽  
Vol 27 (12) ◽  
pp. 1582-1587 ◽  
Author(s):  
K Klaushofer ◽  
H von Mayersbach
Keyword(s):  
Enzyme Activity ◽  
Sensitivity And Specificity ◽  
Rat Liver ◽  
Freeze Substitution ◽  
High Sensitivity ◽  
Histochemical Demonstration ◽  
Frozen Sections ◽  
Enzyme Localization ◽  
Fresh Frozen ◽  
Preparation Techniques

The suitability of freeze-substitution in n-butanol and paraffin embedding of tissues for the histochemical demonstration of 5'-nucleotidase was investigated and compared with commonly used preparation techniques, such as fresh frozen sections and cryostate sections of cold formalin and glutaraldehyde-fixed rat liver. The influences of each step of the preparation techniques on the enzyme activity were controlled by a quantitative radiochemical assay. Freeze substitution was revealed to be superior to the commonly used preparation techniques with respect to: 1) high sensitivity and specificity of the histochemical 5'-nucleotidase reaction (this is based on the fact that incubation media with very low lead concentrations (0,6 mM/1) can be used); 2) excellent morphological appearance of the tissues showing cytological details of enzyme localization; 3) unlimited storage of the tissue materials and ease of sectioning.

Mechanisms by which acute phase proteins enhance development of liver fibrosis: Effects on collagenase and prolyl-4-hydroxylase activity in the rat liver

1986 ◽  
Vol 45 (2) ◽  
pp. 160-170 ◽  
Author(s):  
J. van Gool ◽  
I. de Nie ◽  
J. Smit ◽  
F.M.J. Zuyderhoudt
Keyword(s):  
Liver Fibrosis ◽  
Rat Liver ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Hydroxylase Activity
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