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carp liver
The metabolic thermograms and heat output of mitochondria isolated from carp liver have been determined by using an LKB bioactivity monitor.
      
The metabolites liberated from these glucuronides by the β-glucuronidase treatment could be converted to TA 98 strain mutagens by the carp liver postmitochondrial fraction, but not by the mussel's digestive gland preparation.
      
1).4.TheT* shift in Arrhenius plots following a change in acclimation temperature has been studied for succinate oxidation by carp liver mitochondria (Fig.
      
Neither the function of UCP1, nor the mode of UCP1 activation is known in carp liver mitochondria.
      
coli, brewer's yeast, wheat embryo, carp liver, rabbit liver and rat liver, was performed in a 20% polyacrylamide gel.
      
Inherent in this postulate is the assumption that this minor form of cytochrome P-450 does not contribute significantly to total cytochrome P-450 content of carp liver or 7-ethoxycoumarin-O-deethylase activity.
      
We also made measurements with rat and tench liver, but it has been impossible, under the same experimental conditions, to observe normal release of inorganic phosphorus from G-1-P with carp liver.
      
Preparation of peroxisomes from carp liver by zonal rotor censity gradient centrifugation
      
Peroxisomes from carp liver can be separated by isopycnic density gradient centrifugation in sucrose.
      
The enzyme content of carp liver peroxisomes is similar to that of rat liver, with the exception of α-glycerophosphate dehydrogenase, which in this tissue is a completely soluble cytoplasmic enzyme.
      
The effect of hypoxia (80 pHg) and simultaneously applied paraquat (1,1'-dimethyl-4,4-bipyridynum dichloride) was investigated on carp liver using electron microscopic methods.
      
Variation in the levels of carp liver MDH isozymes may result from the polymorphism of a regulatory mutation affecting isozyme expression, leading to gene silencing after duplication.
      
In carp liver, the percentage of beta endosulfan in the residue decreased with time between exposure and collection of samples whereas the percentage of endosulfan sulphate increased.
      
Some Molecular and Enzymatic Properties of a Homogeneous Preparation of Thiaminase I Purified from Carp Liver
      
A homogeneous preparation of thiaminase I (thiamine:base 2-methyl-4-aminopyrimidine-5-methenyl transferase, EC 2.5.1.2) was obtained from carp liver, for the first time from a nonbacterial source.
      
Carp liver was fractionated by differential and density gradient centrifugation and assayed for enzymes of purine catabolism.
      
As for the gcHIF-4 protein, its expression was also evident in grass carp liver under normoxic condi Phylogenetic Figure 3 Phylogenetic analysis.
      
Carp liver cDNA library was then screened using the 32 P-labeled PCR product as a probe.
      
 

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