Ultrastructural localization of L-?-hydroxy acid oxidase in rat liver peroxisomes

1975 ◽  
Vol 41 (3) ◽  
pp. 195-206 ◽  
Author(s):  
Arthur R. Hand
Keyword(s):  
Rat Liver ◽  
Hydroxy Acid ◽  
Ultrastructural Localization ◽  
Acid Oxidase ◽  
Liver Peroxisomes

scholarly journals THE SYNTHESIS AND TURNOVER OF RAT LIVER PEROXISOMES

1969 ◽  
Vol 41 (2) ◽  
pp. 521-535 ◽  
Author(s):  
Federico Leighton ◽  
Brian Poole ◽  
Paul B. Lazarow ◽  
Christian De Duve
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Isocitrate Dehydrogenase ◽  
Hydroxy Acid ◽  
Deae Cellulose ◽  
Urate Oxidase ◽  
Acid Oxidase ◽  
Total Proteins ◽  
Amino Acid Oxidase ◽  
Liver Peroxisomes

Rat liver peroxisomes isolated by density gradient centrifugation were disrupted at pH 9, and subdivided into a soluble fraction containing 90% of their total proteins and virtually all of their catalase, D-amino acid oxidase, L-α-hydroxy acid oxidase and isocitrate dehydrogenase activities, and a core fraction containing urate oxidase and 10% of the total proteins. The soluble proteins were chromatographed on Sephadex G-200, diethylaminoethyl (DEAE)-cellulose, hydroxylapatite, and sulfoethyl (SE)-Sephadex. None of these methods provided complete separation of the protein components, but these could be distributed into peaks in which the specific activities of different enzymes were substantially increased. Catalase, D-amino acid oxidase, and L-α-hydroxy acid oxidase contribute a maximum of 16, 2, and 4%, respectively, of the protein of the peroxisome. The contribution of isocitrate dehydrogenase could be as much as 25%, but is probably much less. After dissolution of the cores at pH 11 , no separation between their urate oxidase activity and their protein was achieved by Sephadex G-200 chromatography.

scholarly journals Ultrastructural localization of alpha-OH acid oxidase in peroxisomes with the CeCl3 technique.

1980 ◽  
Vol 28 (9) ◽  
pp. 1025-1028 ◽  
Author(s):  
G Arnold ◽  
E Holtzman
Keyword(s):  
Oxidase Activity ◽  
Ultrastructural Localization ◽  
Acid Oxidase ◽  
Cytochemical Method ◽  
Liver Peroxisomes

alpha-OH acid oxidase activity was demonstrated in peroxisomes of glutaraldehyde-fixed tissues using the CeCl3 cytochemical method. For kidney, alpha-OH butyrate or alpha-OH valerate were used as substrates. These substrates gave much less reaction product in liver peroxisomes. Liver peroxisomes were more reactive with glycolate as substrate. Glycolate gave little or no reaction product in kidney peroxisomes. alpha-keto-glutarate inhibited activity of the enzyme with alpha-OH butyrate as substrate.

scholarly journals Ultrastructural localization of catalase and L-alpha-hydroxy acid oxidase in microperoxisomes of Hydra.

1976 ◽  
Vol 24 (8) ◽  
pp. 915-925 ◽  
Author(s):  
A R Hand
Keyword(s):  
Endoplasmic Reticulum ◽  
Lactic Acid ◽  
Hydroxy Acid ◽  
Ultrastructural Localization ◽  
Substrate Oxidation ◽  
Acid Oxidase ◽  
The Matrix ◽  
Acid Reaction ◽  
Cytochemical Reaction ◽  
Glycogen Reaction

The ultrastructural localization of catalase and L-alpha-hydroxy acid oxidase (LalphaHAO) was studied in two species of Hydra. Diaminobenzidine reaction product of catalase activity was present in small round or elongated bodies resembling microperoxisomes in the epitheliomuscular, digestive and gland cells. They were closely related to the endoplasmic reticulum, and were often found in proximity to deposits of lipid and glycogen. Reaction product of LalphaHAO activity was also associated with the microperoxisomes. With rapidly oxidized substrates, such as L-lactic acid, reaction product diffused into the cytoplasm around the microperoxisomes. With slowly oxidized substrates, such as DL-alpha-hydroxyisovaleric acid, reaction product was restricted to the matrix of the microperoxisomes. No reaction product was present in the microperoxisomes in the absence of substrate or with D-lactic acid. The rate of substrate oxidation measured biochemically roughly paralleled the amount of cytochemical reaction product deposited with different substrates. Microperoxisome-like bodies reactive for LalphaHAO were also found in the epidermal cnidoblasts; however, catalase could not be demonstrated in them. This study provides the first cytochemical evidence for the presence of an H2O2-producing oxidase in microperoxisomes.

scholarly journals THE REQUIREMENTS OF THE FATTY ACID OXIDASE COMPLEX OF RAT LIVER

1948 ◽  
Vol 173 (2) ◽  
pp. 753-771 ◽  
Author(s):  
Albert L. Lehninger ◽  
Eugene P. Kennedy
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Acid Oxidase

scholarly journals Cholesterol synthesis in rat liver peroxisomes. Conversion of mevalonic acid to cholesterol.

1987 ◽  
Vol 262 (36) ◽  
pp. 17420-17425 ◽  
Author(s):  
S L Thompson ◽  
R Burrows ◽  
R J Laub ◽  
S K Krisans
Keyword(s):  
Rat Liver ◽  
Cholesterol Synthesis ◽  
Mevalonic Acid ◽  
Liver Peroxisomes

scholarly journals Peroxisomal beta-oxidation. Purification of four novel 3-hydroxyacyl-CoA dehydrogenases from rat liver peroxisomes.

1994 ◽  
Vol 269 (43) ◽  
pp. 27125-27135
Author(s):  
D K Novikov ◽  
G F Vanhove ◽  
H Carchon ◽  
S Asselberghs ◽  
H J Eyssen ◽  
...  
Keyword(s):  
Rat Liver ◽  
Beta Oxidation ◽  
Liver Peroxisomes
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