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Results of the immobilization were evaluated based on analyses of the enzyme activity and stability prior and after immobilization, as well as on the immobilization yield and stability.
Kinetic analyses of the enzyme activity were performed in pooled microsomal samples from colorectal cancer microsomes, healthy colorectal epithelium and human liver microsomes.
Quantitative analyses of the enzyme mRNA expressions (as ratios against respective 18S rRNA) from the paired tissues (tumor and nontumor [normal]) from the 11 patients are shown in Table 2. Tissues from 11/11 patients showed higher levels of 5αR1 (SRD5A1) expression in tumor than in the normal tissue.
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Evolutionary analyses of the enzymes catalyzing the kynurenine pathway (fig. 6 and supplementary figs. S3 S6, Supplementary Material online) currently do not support horizontal gene transfer from eukaryotes into Xanthomonadales, Flavobacteriales, or other bacterial lineages.
In order to determine the origin of mitochondria-targeted enzymes found in Euglena and to investigate the relationships of the enzymes found in other eukaryotes, particularly to determine if isoforms found in the cytosol of aplastidic eukaryotes are related to those found in plastids, we performed phylogenetic analyses of the enzymes of the pathway.
Phylogenetic and bipartition analyses of the enzymes involved in cytoplasmic steps (MurA, MurB, MurCDEF, Ddl, and MurI) identified an Aquificae cohesive clan adjacent to the Epsilonproteobacteria in the trees of MurA, B, and I, whereas the Mur ligases MurCD and MurEF, and Ddl were adjacent to the Thermotogae.
The subsequent analyses of these enzymes uncovered a key role for excessive cathepsin K activity in the cartilage lesions noted in ML-II embryos.
Subsequent comparative sequence and structural analyses of the associated enzymes reveal potential homology.
The identification and subsequent analyses of the FDL enzymes has clearly shown that they play a role in N-glycan maturation in many invertebrates (Léonard et al. 2006; Rendic et al. 2008; Geisler and Jarvis 2012).
Phylogenetic analyses of the constituent enzymes from this widely conserved pathway (Mamat et al. 2009; Wang and Quinn 2010) were consistent with exclusive epsilonproteobacterial affiliations identified in previous studies (Plötz et al. 2000; Cavalier-Smith 2002; Beiko et al. 2005).
Immunohistochemical and biochemical analyses show localization of the enzyme and its oxidation products within human atherosclerotic lesions (Hazen and Heinecke, 1997; Sugiyama et al., 2001; Hazell et al., 2001; Thukkani et al., 2003).
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