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JournalISSN: 1096-4959

Comparative Biochemistry and Physiology B 

Elsevier BV
About: Comparative Biochemistry and Physiology B is an academic journal published by Elsevier BV. The journal publishes majorly in the area(s): Fatty acid & Amino acid. It has an ISSN identifier of 1096-4959. Over the lifetime, 12650 publications have been published receiving 253305 citations. The journal is also known as: Comparative Biochemistry and Physiology. Part B: Biochemistry & Molecular Biology & Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.
Topics: Fatty acid, Amino acid, Enzyme, Gene, Peptide sequence


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Journal ArticleDOI
TL;DR: Results of studies on the energy requirements of fish during recent years have indicated that in the carnivorous fish such as rainbow trout, eel, yellowtail and plaice which have limited ability to utilize carbohydrates of high mol, dietary lipids play an important role in this respect and have a sparing action on dietary protein.
Abstract: Dietary lipids play important roles in the energy production processes of animal tissues and as the source of essential fatty acids (EFA). Besides these functions they do have other important dietary roles as carriers of certain non-fat nutrients, notably the fat-soluble vitamins A, D and K. Recent studies on EFA in fish have demonstrated that EFA requirements of fish differ considerably from species to species. On the other hand, the results of studies on the energy requirements of fish during recent years have indicated that in the carnivorous fish such as rainbow trout, eel, yellowtail and plaice which have limited ability to utilize carbohydrates of high mol. wt as an energy source, dietary lipids play an important role in this respect and have a sparing action on dietary protein.

929 citations

Journal ArticleDOI
TL;DR: An outline of the current state of arginase research is presented by giving a comparative overview ofArginases and their associated properties by way of comparison with previous work.
Abstract: Arginase is a primordial enzyme, widely distributed in the biosphere and represented in all primary kingdoms. It plays a critical role in the hepatic metabolism of most higher organisms as a cardinal component of the urea cycle. Additionally, it occurs in numerous organisms and tissues where there is no functioning urea cycle. Many extrahepatic tissues have been shown to contain a second form of arginase, closely related to the hepatic enzyme but encoded by a distinct gene or genes and involved in a host of physiological roles. A variety of functions has been proposed for the “extrahepatic” arginases over the last three decades. In recent years, interest in arginase has been stimulated by a demonstrated involvement in the metabolism of the ubiquitous and multifaceted molecule nitric oxide. Molecular biology has begun to furnish new clues to the disparate functions of arginases in different environments and organisms. Comparative studies of arginase sequences are also beginning to elucidate the comparative evolution of arginases, their molecular structures and the nature of their catalytic mechanism. Further studies have sought to clarify the involvement of arginase in human disease. This review presents an outline of the current state of arginase research by giving a comparative overview of arginases and their associated properties.

575 citations

Performance
Metrics
No. of papers from the Journal in previous years
YearPapers
202324
2022119
2021102
202087
2019102
201878