scholarly journals MetaBridge: An Integrative Multi‐Omics Tool for Metabolite‐Enzyme Mapping

2020 ◽  
Vol 70 (1) ◽  
Author(s):  
Travis Blimkie ◽  
Amy Huei‐Yi Lee ◽  
Robert E.W. Hancock
Keyword(s):  

1990 ◽  
Vol 18 (3) ◽  
pp. 144-146 ◽  
Author(s):  
Stephen J Higgins ◽  
B David Hames ◽  
Elizabeth McIntosh ◽  
Alan Colman


2021 ◽  
Vol 888 (1) ◽  
pp. 012024
Author(s):  
P W Prihandini ◽  
A Primasari ◽  
M Luthfi ◽  
D Pamungkas ◽  
A P Z N L Sari ◽  
...  

Abstract The restriction enzyme is important for genotyping using the PCR-RFLP technique. Therefore, this study aims to identify the restriction enzyme mapping in the partial sequence of the follicle-stimulating hormone receptor (FSHR) gene in Indonesian local cattle. A total of 29 samples sized 306 bp, were aligned with Genbank sequence acc no. NC_032660, resulting three polymorphic sites, namely g.193G>C, g.227T>C, and g.275A>C. Furthermore, the restriction mapping analysis using the NEBcutter program V2.0 showed that no enzyme recognized the SNP g.275A>C, while the SNP g.193G>C and g.227T>C were identified by the AluI and MscI enzymes, respectively. The AluI enzyme cuts at two positions (193 bp and 243 bp) in the G allele sample producing three fragments namely 50 bp, 63 bp, and 193 bp, meanwhile, in the C allele, the AluI cuts only in position 243 bp, hence, the fragment products are 63 bp and 243 bp. In contrast, the MscI enzyme was only recognized in the T allele, producing fragments sized 77 bp and 229 bp but failed to identify the restriction site along with the PCR products in the C allele. Based on the results, the SNPs (g.193G>C and g.227T>C) and restriction enzymes (AluI and MscI) are applicable for genotyping local Indonesian cattle using the PCR-RFLP technique in future studies.



Genetics ◽  
1991 ◽  
Vol 128 (3) ◽  
pp. 529-538 ◽  
Author(s):  
G May ◽  
L Le Chevanton ◽  
P J Pukkila

Abstract We report here the molecular cloning of the A43 mating type factor from Coprinus cinereus, a basidiomycetous fungus. Our molecular analyses revealed an unexpected source of variation in the A factor. Though genetic studies have demonstrated that A has two subunits, alpha and beta, we located three nonoverlapping fragments in the A43 region that have A factor function following DNA-mediated transformation. The three fragments demonstrate no similarity to one another as judged by restriction enzyme maps and by hybridization on Southern blots. We conclude that the A43 factor is composed of at least three subunits. When strains carrying different A factors are examined by hybridization to the cloned subunits, extensive polymorphism is seen. Both intensity of hybridization and restriction fragment lengths vary between strains. Some strains fail to show any hybridization to a probe. In contrast, other strains from widely separated geographic locations apparently share very similar subunits. From comparative restriction enzyme mapping of A43 and a mutated A43 factor, we inferred that a 12-kb deletion in the A factor was responsible for the constitutive, dominant phenotype of the mutated A factor. The results of transformation experiments support an activator model for the activity of the A factor in regulating the A pathway.



1986 ◽  
Vol 164 (1) ◽  
pp. 345-350 ◽  
Author(s):  
B S Nepom ◽  
J Palmer ◽  
S J Kim ◽  
J A Hansen ◽  
S L Holbeck ◽  
...  

HLA-DR4, Dw4-associated haplotypes associated with IDDM and JRA were compared using genomic DNA restriction fragment analysis to distinguish among DQ beta and alpha alleles linked to DR4. DQ beta polymorphisms that subdivide the HLA-DQw3 specificity into DQ3.1 and 3.2 alleles were identified. More than 90% of DR4+ IDDM patients express one of these alleles, DQ3.2; restriction enzyme mapping indicates that the presence of this allele also accounts for the genomic fragment patterns previously reported in IDDM. Furthermore, haplo-identical siblings of DQ3.2 IDDM patients also carry the DQ3.2 allele, regardless of clinical presentation. In contrast, DR4+ JRA patients show no allelic preference at DQ beta, implicating different HLA genetic contributions in these two DR4-associated diseases.



2003 ◽  
Vol 285 (1) ◽  
pp. L149-L160 ◽  
Author(s):  
Lubna H. Abdullah ◽  
Jason T. Bundy ◽  
Camille Ehre ◽  
C. William Davis

SPOC1 cells, which are a mucin-secreting model of rat airway goblet cells, possess a luminal P2Y2 purinoceptor through which UTP, ATP, and ATPγS stimulate secretion with EC50 values of ∼3 μM. PMA elicits mucin secretion with high EC50 (75 nM) and saturation (300 nM) values. For the first time in airway mucin-secreting cells, the PKC isoforms expressed and activated by a secretagogue were determined using RT-PCR/restriction-enzyme mapping and Western blotting. Five isoforms were expressed: cPKCα, nPKCδ and -η, and aPKCζ and -ι/λ. PMA caused cPKCα and nPKCδ to translocate to the membrane fraction of SPOC1 cells; only nPKCδ so responded to ATPγS. Membrane-associated nPKCδ and mucin secretion increased in parallel with ATPγS concentration and yielded EC50 values of 2–3 μM and maximum values of 100 μM. Effects of PMA to increase membrane-associated cPKCα and nPKCδ saturated at 30 nM, whereas mucin secretion saturated at 300 nM, which suggests a significant PKC-independent effect of PMA on mucin secretion. A prime alternate phorbol ester-receptor candidate is the C1-domain protein MUNC13. RT-PCR revealed the expression of ubiquitous (ub)MUNC13-2 and its binding partner, DOC2-γ. Hence, P2Y2 agonists activate nPKCδ in SPOC1 cells. PMA activates cPKCα and nPKCδ at high affinity and stimulates a lower affinity PKC-independent pathway that leads to mucin secretion.



1992 ◽  
Vol 10 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Michael A. Mallamaci ◽  
David P. Reed ◽  
Stephen A. Winkle


1991 ◽  
Vol 46 (2) ◽  
pp. 275-284 ◽  
Author(s):  
Harry van Keulen ◽  
Scott R. Campbell ◽  
Stanley L. Erlandsen ◽  
Edward L. Jarroll




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