Kinetics of the Thermal Inactivation of Alkaline Phosphatase from Green Crab(Scylla Serrata)

Chen, Qing‐Xi; Zhang, Wei; Yan, Si-Xu; Zhang, Tong; Zhou, Hai‐Meng

doi:10.3109/14756369709035813

Cited by 6 publications

(2 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5). The inhibition of the AP activities of chela muscle of C. granulatus at high temperatures is similar to that described for AP purified from viscera of Pinctada fucata (Xiao et al, 2002) and from the digestive tract of S. serrata (Chen et al, 1997). Since C. granulatus in Mar Chiquita coastal lagoon is exposed to frequent changes in the environmental temperature, the differential sensitivity to temperature of these AP activities could be associated with a distinct role in thermal acclimation.…”

Section: Discussionsupporting

confidence: 74%

Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity

Pinoni

Goldemberg

Mañanes

2005

Journal of Experimental Marine Biology and Ecology

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 74%

Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity

Pinoni

Goldemberg

Mañanes

2005

Journal of Experimental Marine Biology and Ecology

View full text Add to dashboard Cite

“…7) is in agreement with that found for this activity in chela muscle of C. granulatus (Pinoni et al, 2005). an inhibition of aP activity at high temperatures has also been described for AP purified from viscera of P. fucata (Xiao et al, 2002) and from the digestive tract of S. serrata (Chen et al, 1997).…”

Section: Atpase and Levamisole-sensitive Ap Activity Of Muscle Of Cyrmentioning

confidence: 75%

Caracterización parcial y respuesta bajo condiciones de hiperregulación de las actividades de Na+-K+ ATPasa y fosfatasa alcalina levamisol-sensible en músculo de la quela del cangrejo eurihalino Cyrtograpsus angulatus

Pinoni¹,

Mañanes²

2008

Sci. Mar.

View full text Add to dashboard Cite

SUMMary: the occurrence, characteristics and response to changes in environmental salinity of na + -K + atPase and levamisole-sensitive alkaline phosphatase (aP) activities were studied in chela muscle of the euryhaline crab Cyrtograpsus angulatus. Chela muscle exhibited an na + -K + atPase activity which was strongly dependent on atP concentration, pH and temperature of the reaction mixture. Maximal activity was found at 1 mM atP, 30-37ºC and pH 7.4. levamisole-sensitive aP activity was characterised at physiological pH 7.4 and at pH 8.0. i 50 for levamisole-sensitive aP activity was 8.8 mM and 8.0 mM at pH 7.4 and 8.0, respectively. at both pH levels, levamisole-sensitive aP activity exhibited Michaelis-Menten kinetics (K m =3.451 mM and 6.906 mM at pH 7.4 and 8.0, respectively). levamisole-sensitive aP activities were strongly affected by temperature, exhibiting a peak at 37ºC. in crabs acclimated to low salinity (10; hyperegulating conditions), na + -K + atPase activity and levamisole-sensitive aP activity at the physiological pH were higher than in 35 psu (osmoconforming conditions). the response to low salinity suggests that both activities could be components of muscle regulatory mechanisms at the biochemical level secondary to hyperegulation of C. angulatus. the study of these activities under hyperegulating conditions contributes to a better understanding of the complexity of biochemical mechanisms underlying the adaptive process of euryhaline crabs.Keywords: alkaline phosphatase, na + -K + atPase, crabs, Cyrtograpsus angulatus, levamisole, muscle.reSUMen: CaraCterizaCión parCial y respuesta bajo CondiCiones de hiperregulaCión de las aCtividades de na + -K + atpasa y fosfatasa alCalina levamisol-sensible en músCulo de la quela del Cangrejo eurihalino Cyrtograpsus angulatus. -en el presente trabajo se estudió la presencia, características y respuesta a la salinidad ambiental de las actividades de na + -K + atPasa y fosfatasa alcalina (aP) levamisol-sensible en el músculo de la quela del cangrejo eurihalino Cyrtograpsus angulatus. el músculo de la quela exhibió una actividad de na + -K + atPasa marcadamente dependiente de la concentración de atP, pH y temperatura del medio de reacción. la actividad fue máxima a 1 mM de atP, 30-37ºC y a pH 7.4. la actividad de AP levamisol-sensible se caracterizó parcialmente a pH fisiológico (pH 7.4) y a pH 8.0. La I 50 fue de 8.8 y 8.0 mM de levamisol a pH 7.4 y 8.0 respectivamente. a ambos pH la actividad de aP levamisol-sensible exhibió una cinética michaeliana (K m =3.451 y 6.606 mM de pnPP, respectivamente). las actividades de aP levamisol-sensibles fueron fuertemente afectadas por la temperatura, exhibiendo un pico a 37ºC. en cangrejos aclimatados a baja salinidad (10) (condiciones de hiperregulación), las actividades de na + -K + ATPasa y de AP levamisol-sensible a pH fisiológico fueron mayores que a 35 de salinidad (condiciones de osmoionoconformación). la respuesta a baja salinidad sugiere que ambas actividades serían componentes de los mecanismos regulatorios a ...

show abstract

Irreversible kinetics of β-N-acetyl-d-glucosaminidase from prawn (Penaeus vannamei) inactivated by mercuric ion

Lin

Chen

Xie

et al. 2006

Journal of Experimental Marine Biology and Ecology

View full text Add to dashboard Cite

Kinetics of the Thermal Inactivation of Alkaline Phosphatase from Green Crab(Scylla Serrata)

Cited by 6 publications

References 9 publications

Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity

Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity

Caracterización parcial y respuesta bajo condiciones de hiperregulación de las actividades de Na<sup>+</sup>-K<sup>+</sup> ATPasa y fosfatasa alcalina levamisol-sensible en músculo de la quela del cangrejo eurihalino <i>Cyrtograpsus angulatus</i>

Irreversible kinetics of β-N-acetyl-d-glucosaminidase from prawn (Penaeus vannamei) inactivated by mercuric ion

Contact Info

Product

Resources

About