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Digitale Medien

An ice nucleation active gene of Erwinia ananas - Sequence similarity to those of Pseudomonas species and regions required for ice nucleation activity

Abe, K. ; Watabe, S. ; Emori, Y. ; [weitere]

Amsterdam : Elsevier

FEBS Letters 258 (1989), S. 297-300

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ISSN: 0014-5793

Schlagwort(e): Erwinia ananas ; Ice nucleation gene ; Repetition sequence ; inaA ; inaZ

Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Thema: Biologie , Chemie und Pharmazie , Physik

Materialart: Digitale Medien

URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(89)81678-3

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Digitale Medien

Changes in carp myosin ATPase induced by temperature acclimation (1990)

Hwang, G. C. ; Watabe, S. ; Hashimoto, K.

Springer

Journal of comparative physiology 160 (1990), S. 233-239

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ISSN: 1432-136X

Schlagwort(e): Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Summary Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold-and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·mg-1 at pH 9. K+(EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 μmol Pi·min-1·mg-1 at 0.6–0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold-and warm-acclimated carp. The maximum initial velocity was 0.53 μmol Pi·min-1·mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25·10-4·s-1 at 30°C and pH 7.0 for cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00302588

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Digitale Medien

Subunit structures of multiple hemoglobins in carp (1993)

Ohkubo, N. ; Watabe, S. ; Oshiro, T. ; [weitere]

Springer

Journal of comparative physiology 163 (1993), S. 445-451

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ISSN: 1432-136X

Schlagwort(e): Multiple hemoglobins ; Subunit structure ; α-chain ; β-chain ; Carp, Cyprinus carpio

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Abstract Three hemoglobin components in carp designated CI, CII, and CIII, were isolated by DEAE-Toyopearl ion-exchange chromatography. Constituent globin chains, α1, α2, β1 and β2, were analyzed by urea-Triton acid polyacrylamide gel electrophoresis and isolated by high performance liquid chromatography with a reversed-phase column. Tryptic peptide mapping indicated that the α-globin chains of the three hemoglobin components have slightly different structures. In addition, N-terminal amino acid sequence analysis indicated that the β1-globin chain has a primary structure different from that of the β2-chain. A series of hybridization experiments between isolated hemoglobins, together with such structural properties of globin chains, suggested that the three hemoglobins have the following compositions: CI (α1 α2 β 2 1 ), CII (α1 α2 β1 β2), and CIII (α1 α2 β 2 2 ). Hemoglobin CII was a hybrid between the two types each of α- and β-chain and could be constructed in vitro from two hemoglobin components CI and CIII.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00346928

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