Adaptative features of ectothermic enzymes-IV. Studies on malate dehydrogenase of Astyanax fasciatus (Characidae) from lobo reservoir (Sao Carlos, Sao Paulo, Brasil)

1. Skeletal muscle and heart supernatant malate dehydrogenase (s-MDH) from a subtropical fish, Astyanax fasciatus consists of three electrophoretically anodal bands. Each band is a dimer (AA, AB and BB) and two loci are active.2. In A. fasciatus tissue extracts, A and B subunits are present at diffe... Ausführliche Beschreibung

1. Person: De Luca, P.H.
Weitere Personen: Schwantes, M.L.B.; Schwantes, A.R.
Quelle: in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Vol. 74, No. 2 (1983), p. 315-324
Weitere Artikel
Format: Online-Artikel
Sprache: English
Veröffentlicht: 1983
Beschreibung: Online-Ressource
Online Zugang: Online
Volltext
Tags: Hinzufügen
Keine Tags. Fügen Sie den ersten Tag hinzu!
Anmerkung: Copyright: Copyright (c) 2002 Elsevier Science Inc.
LEADER 02271nma a2200337 c 4500
001 NLEJ187182116
003 DE-601
005 20151015034025.0
007 cr uuu---uuuuu
008 070506s1983 000 0 eng d
016 7 |a 1481604-0  |2 DE-600 
024 8 |a 0305-0491(83)90019-6 
035 |a (DE-599)GBVNLZ187182116 
040 |b ger  |c GBVCP 
041 0 |a eng 
084 |a sdj  |2 natliz 
245 0 0 |a Adaptative features of ectothermic enzymes-IV. Studies on malate dehydrogenase of Astyanax fasciatus (Characidae) from lobo reservoir (Sao Carlos, Sao Paulo, Brasil)  |h Elektronische Ressource 
300 |a Online-Ressource 
500 |a Copyright: Copyright (c) 2002 Elsevier Science Inc. 
520 |a 1. Skeletal muscle and heart supernatant malate dehydrogenase (s-MDH) from a subtropical fish, Astyanax fasciatus consists of three electrophoretically anodal bands. Each band is a dimer (AA, AB and BB) and two loci are active.2. In A. fasciatus tissue extracts, A and B subunits are present at differing quantitative levels and their activities are almost season-independent. However, the relative activity of each homodimer in relation to total s-MDH estimated by densitometry of gels or of each homodimer purified by chromatography varies with temperature. The more anodic homodimer is termolabile and the less anodic one is thermostable.3. The pH optimum of s-MDH is 7.5, of AA is 6.5 and of BB is 7.8.4. The BB isozyme is more sensitive to high concentrations of substrate and has a K"m temperature-independent. The AA isozyme is not inhibited by high concentrations of oxaloacetate and shows a K"m temperature-dependent with a fourteenfold increase between 20^o and 40^oC. 
533 |a Online edition  |f Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 ; 041023-8 
700 1 |a De Luca, P.H. 
700 1 |a Schwantes, M.L.B. 
700 1 |a Schwantes, A.R. 
773 0 8 |i in  |t Comparative Biochemistry and Physiology -- Part B: Biochemistry and  |d Amsterdam : Elsevier  |g Vol. 74, No. 2 (1983), p. 315-324  |q 74:2<315-324  |w (DE-601)NLEJ177069775  |x 0305-0491 
856 4 0 |u http://linkinghub.elsevier.com/retrieve/pii/0305-0491(83)90019-6 
901 |a OLC 
912 |a ZDB-1-SDJ 
912 |a GBV_NL_ARTICLE 
951 |a AR 
952 |d 74  |j 1983  |e 2  |h 315-324 

Ähnliche Einträge

Keine ähnlichen Titel gefunden

Privacy Notice Ask a Librarian New Acquisitions