scholarly journals Molecular Characterization of the Gerbil C5a Receptor and Identification of a Transmembrane Domain V Amino Acid That Is Crucial for Small Molecule Antagonist Interaction

2005 ◽  
Vol 280 (49) ◽  
pp. 40617-40623 ◽  
Author(s):  
Stephen M. Waters ◽  
Robbin M. Brodbeck ◽  
Jeremy Steflik ◽  
Jianying Yu ◽  
Carolyn Baltazar ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Small Molecule ◽  
Transmembrane Domain ◽  
C5a Receptor ◽  
Small Molecule Antagonist ◽  
Domain V

scholarly journals Molecular characterization of Prunus necrotic ringspot virus isolated from rose in Brazil

2015 ◽  
Vol 45 (12) ◽  
pp. 2197-2200 ◽  
Author(s):  
Thor Vinícius Martins Fajardo ◽  
Monique Bezerra Nascimento ◽  
Marcelo Eiras ◽  
Osmar Nickel ◽  
Gilvan Pio-Ribeiro
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Molecular Analysis ◽  
Nucleotide Sequences ◽  
Amino Acid Sequences ◽  
Causal Agent ◽  
Ringspot Virus ◽  
Prunus Necrotic Ringspot Virus ◽  
First Time

ABSTRACT: There is no molecular characterization of Brazilian isolates of Prunus necrotic ringspot virus (PNRSV), except for those infecting peach. In this research, the causal agent of rose mosaic was determined and the movement (MP) and coat (CP) protein genes of a PNRSV isolate from rose were molecularly characterized for the first time in Brazil. The nucleotide and deduced amino acid sequences of MP and CP complete genes were aligned and compared with other isolates. Molecular analysis of the MP and CP nucleotide sequences of a Brazilian PNRSV isolate from rose and others from this same host showed highest identities of 96.7% and 98.6%, respectively, and Rose-Br isolate was classified in PV32 group.

scholarly journals Morphology and molecular characterization of newly isolated microalgae strain Chlorella volutis LIPI13-WKT066 from Wakatobi Islands and its potential use

2019 ◽  
Vol 23 (1) ◽  
pp. 13
Author(s):  
Delicia Yunita Rahman ◽  
Swastika Praharyawan ◽  
Sapto Raharjo ◽  
Farizul Fadiyah ◽  
Dwi Susilaningsih
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Acid Content ◽  
National Park ◽  
Amino Acid Content ◽  
Morphological Observation ◽  
Future Application ◽  
Health Application ◽  
Potential Use

Morphology and molecular characterization of microalgae isolated from Wakatobi Marine National Park was conducted. An understanding of the characteristics of morphology, molecular, as well as metabolites profile of the microalgae species is potentially useful for its future application. The primary aim of this study was to isolate, identify and characterize the microalgae strain isolated from Wakatobi Marine National Park labeled as LIPI13-WKT066 with the emphasis on the evaluation of amino acid content as a basis for its health application. Morphological observation under the microscope and molecular identification suggested that the microalgae strain of LIPI13-WKT066 belong to the strain under species of Chlorella volutis. Metabolite characterization of the microalgae strain showed that the content of protein (11.9%), lipid (12.4%) and carbohydrate (4.7%) was in the regular range. Further analysis of its amino acid content revealed the potency of the microalgae strain to be used as antihypertensive agent.

Molecular Characterization of Genes Coding for Wild-Type and Sulfonylurea-Resistant Acetolactate Synthase in the Cyanobacterium Synechococcus PC C7942

1990 ◽  
Vol 45 (5) ◽  
pp. 538-543 ◽  
Author(s):  
D. Friedberg ◽  
J. Seijffers
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Characterization ◽  
Amino Acid Level ◽  
Acetolactate Synthase ◽  
Mutant Gene ◽  
Wild Type ◽  
E Coli

We present here the isolation and molecular characterization of acetolactate synthase (ALS) genes from the cyanobacterium Synechococcus PCC7942 which specify a sulfonylurea-sensitive enzyme and from the sulfonylurea-resistant mutant SM3/20, which specify resistance to sulfonylurea herbicides. The ALS gene was cloned and mapped by complementation of an Escherichia coli ilv auxotroph that requires branched-chain amino acids for growth and lacks ALS activity. The cyanobacterial gene is efficiently expressed in this heterologous host. The ALS gene codes for 612 amino acids and shows high sequence homology (46%) at the amino acid level with ALS III of E. coli and with the tobacco ALS. The resistant phenotype is a consequence of proline to serine substitution in residue 115 of the deduced amino acid sequence. Functional expression of the mutant gene in wild-type Synechococcus and in E. coli confirmed that this amino-acid substitution is responsible for the resistance. Yet the deduced amino-acid sequence as compared with othjer ALS proteins supports the notion that the amino-acid context of the substitution is important for the resistance.

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