The soluble carnitine palmitoyltransferase from bovine liver. A comparison with the enzymes from peroxisomes and from the mitochondrial inner membrane.

TL;DR: The use of total volatile basic nitrogen (TVB-N) as a quality parameter for fish is rapidly growing to include other types of meat, but little is known on the biochemical pathways involved in its generation.

TL;DR: It is suggested that malonyl-CoA inhibition of the peroxisomal enzyme as well as of the mitochondrial enzyme is important for the regulation of mitochondrial fatty acid oxidation.

TL;DR: The results of the combined studies using both diet and drugs to cause enzyme induction suggest that the synthesis of the carnitine acyltransferases (mitochondrial CPT and peroxisomal CPTs) may be co-ordinated with each other; however, the co-ordinate regulatory factors have not yet been identified.

Abstract: Numerous investigators have studied monoamine oxidase since it was first described (2) in 1928. The literature has recently been reviewed by Blaschko (3) and Zeller (4). Monoamine oxidase has usually been considered as a single enzyme (5), but some authors (Werle and Roewer (6) and Alles and Heegaard (7)) have presented evidence indicating that these preparations contained more than one type of amine oxidase activity. All of these studies, however, have been carried out with relatively crude preparations, since monoamine oxidase is associated with particulate material and has resisted efforts to purify it. Although many tissues were found to contain this activity, liver preparations have been most commonly used. Amine oxidase activity has been reported to be present in dog blood by Werle and Roewer (6), but has usually been considered to be absent in the blood of other species (3). Although Hirsch (8) reported the oxidation of spermine and spermidine by beef and sheep serum, no significant activity Tvas observed with those monoamines and diamines tested. In the present work a soluble amine oxidase has been purified 150to 200fold from steer plasma; the enzyme oxidatively deaminates a variety of amines with the stoichiometric formation of the corresponding aldehydes, ammonia, and hydrogen peroxide. The substrate and inhibitor specificities of this enzyme differ markedly from those described for the liver preparations.

TL;DR: Findings show that whereas the malonyl-CoA binding site relevant to the inhibition of carnitine palmitoyltransferase is situated on the outer side of the outer membrane, the overt carnitinespeciespecies activity resides on the inner side ofThe outer membrane.