scholarly journals The effect of temperature on catalytic and regulatory functions of pyruvate kinases of the rainbow trout and the Antarctic fish Trematomus bernacchii

1968 ◽  
Vol 110 (3) ◽  
pp. 395-400 ◽  
Author(s):  
G. N. Somero ◽  
P. W. Hochachka
Keyword(s):  
Rainbow Trout ◽  
Pyruvate Kinase ◽  
Feedback Inhibition ◽  
Antarctic Fish ◽  
Effect Of Temperature ◽  
Km Value ◽  
Trematomus Bernacchii ◽  
Regulatory Functions ◽  
Pyruvate Kinases ◽  
The Antarctic

1. The effects of temperature on the catalytic and regulatory properties of pyruvate kinases from the temperate-zone rainbow trout and the Antarctic fish Trematomus bernacchii were examined. 2. The Km value of pyruvate kinase for one of its two substrates, phosphoenolpyruvate, is temperature-dependent, and is lowest at temperatures that closely coincide with the habitat temperatures of the two fishes. 3. Two regulatory functions of pyruvate kinase, feedforward activation by fructose diphosphate and feedback inhibition by ATP, are temperature-independent. Enzyme–ADP interaction is also temperature-independent. 4. It is concluded that enzyme–substrate and enzyme–modulator interactions are important factors in short-term and in evolutionary adaptations by poikilotherms to changes in temperature. Though the Km for substrate may vary in apparently adaptive manners, the regulatory functions of an enzyme appear to be unchanged over the range of temperatures experienced by the organism in Nature.

scholarly journals INFLUÊNCIA DA TEMPERATURA E DO pH NAS PROPRIEDADES CINÉTICAS DA LACTATO DESIDROGENASE DO MÚSCULO EPAXIAL DE Prochilodus scropha e Notothenia neglecta

1998 ◽  
Vol 3 (1) ◽  
Author(s):  
CLEONI SANTOS CARVALHO ◽  
RUBENS ROSA ◽  
KIKUE T. SASSAKI ◽  
METRY BACILA
Keyword(s):  
Lactate Dehydrogenase ◽  
Ph Effect ◽  
Antarctic Fish ◽  
Tropical Fish ◽  
Effect Of Temperature ◽  
Kinetic Properties ◽  
Activation Effect ◽  
Nad Oxidoreductase ◽  
The Antarctic ◽  
Epaxial Muscle

Foi levado a efeito um estudo comparativo das propriedades cinéticas da lactico desidrogenase (Llactato NAD+ oxidorreductase, E.C.1.1.1.27) purificada do músuclo epaxial do peixe tropical Prochilodus scropha e do peixe antártico Notothenia neglecta. Os seguintes parâmetros foram estudados: a. Efeito do pH; efeito da temperatura e valores para a energia de ativação; efeito da concentração de substrato e o efeito da temperatura sobre os valores de Km. Abstract It has been carried out a comparative study on the kinetic properties of the lactate dehydrogenase (L-lactate NAD+ oxidoreductase, E.C.1.1.1.27) purified from the epaxial muscle of the tropical fish Prochilodus scropha and the Antarctic fish Notothenia neglecta. The following parameters were studied: a. Effect of pH; effect of temperature and values for energy of activation; effect of substrate concentration and the effect of temperature on the Km values.

Vitellogenin gene expression in males of the Antarctic fish Trematomus bernacchii from Terra Nova Bay (Ross Sea): A role for environmental cadmium?

Chemosphere ◽  
2007 ◽  
Vol 66 (7) ◽  
pp. 1270-1277 ◽  
Author(s):  
Adriana Canapa ◽  
Marco Barucca ◽  
Stefania Gorbi ◽  
Maura Benedetti ◽  
Sara Zucchi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Ross Sea ◽  
Antarctic Fish ◽  
Terra Nova Bay ◽  
Trematomus Bernacchii ◽  
Terra Nova ◽  
Vitellogenin Gene ◽  
The Antarctic

Characterization and expression of a new cytoplasmic glutathione peroxidase 1 gene in the Antarctic fish Trematomus bernacchii

Hydrobiologia ◽  
2015 ◽  
Vol 761 (1) ◽  
pp. 363-372 ◽  
Author(s):  
G. Sattin ◽  
R. Bakiu ◽  
A. M. Tolomeo ◽  
A. Carraro ◽  
D. Coppola ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Antarctic Fish ◽  
Glutathione Peroxidase 1 ◽  
Trematomus Bernacchii ◽  
The Antarctic

Olfactory search tracks in the Antarctic fish Trematomus bernacchii

Polar Biology ◽  
1999 ◽  
Vol 21 (3) ◽  
pp. 151-154 ◽  
Author(s):  
John C. Montgomery ◽  
Carol Diebel ◽  
Matthew B. D. Halstead ◽  
Josh Downer
Keyword(s):  
Antarctic Fish ◽  
Trematomus Bernacchii ◽  
The Antarctic

scholarly journals Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity

2019 ◽  
Vol 9 (20) ◽  
pp. 4299 ◽  
Author(s):  
Shweta Borkar ◽  
Sondavid Nandanwar ◽  
Jun Lee ◽  
Hak Kim
Keyword(s):  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Antarctic Fish ◽  
Effect Of Temperature ◽  
Dissostichus Mawsoni ◽  
Sytox Green ◽  
Uptake Assay ◽  
The Antarctic ◽  
Β Sheet

Liver-expressed antimicrobial peptides (LEAPs) are cysteine-containing cationic peptides. LEAP-1 and LEAP-2 are eight- and four-cysteine containing antimicrobial peptides found in animals, respectively. LEAP-1 is widely known as antibacterial peptide involved in the innate immunity of fish, but the roles of LEAP-1 and LEAP-2 in Antarctic fish species are unknown. In the present study, we synthesized and characterized novel LEAPs with four and eight cysteine residues, derived from Antarctic notothenioid (Dissostichus mawsoni) and Antarctic eelpout (Lycodichthys dearborni). Circular dichroism spectroscopy of these peptides showed a typical β-sheet conformation. The LEAPs were found to be bactericidal against gram-positive as well as gram-negative bacteria. In the SYTOX green uptake assay, LEAPs did not trigger any significant increase in fluorescence. However, LEAPs competitively bound to DNA and replaced the ethidium bromide (EB) dye. To determine the effect of temperature on the activity of LEAPs, we evaluated the antibacterial activity against Listeria monocytogenes at 5, 15, 25, and 35 °C. The results showed that the antibacterial activity of LEAPs increased with a decrease in temperature, which may indicate that the Antarctic fish LEAP are evolutionarily adapted. Taken together, our results suggest that novel Antarctic LEAPs are bactericidal peptides with the likely mode of action being DNA binding and may be evolved to adapt to cold temperature.

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