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guanine/soya

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NakalaMajaribio ya klinikiHati miliki
5 matokeo

Target Specificity of the CRISPR-Cas9 System in Arabidopsis thaliana, Oryza sativa, and Glycine max Genomes.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
Clustered regularly interspaced short palindromic repeats (CRISPR), a class of immune-associated sequences in bacteria, have been developed as a powerful tool for editing eukaryotic genomes in diverse cells and organisms in recent years. The CRISPR-Cas9 system can recognize upstream 20 nucleotides

NADH Oxidase Activity of Plasma Membranes of Soybean Hypocotyls Is Activated by Guanine Nucleotides.

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
The activity of an auxin-stimulated NADH oxidase of the plasma membrane of hypocotyls of etiolated soybean (Glycine max Merr.) seedlings responded to guanine and other nucleotides, but in a manner that differed from that of enzymes coupled to the classic trimeric and low molecular weight monomeric
We have isolated a cDNA clone from Glycine max, named SGA2, coding for a G alpha-subunit protein. The encoded polypeptide, SG alpha2, shows a molecular mass of 45 kDa and contains most of the conserved regions involved in guanine nucleotide binding and hydrolysis. Comparison at the nucleotide and
The sucrose binding protein (SBP) has been implicated as an important component of the sucrose uptake system in plants. SBP-mediated sucrose transport displays unique kinetic features and the protein is not similar to other transport proteins. Here, we report the characterization of a member of the

Adenine binding sites of the lectin from lima beans (Phaseolus lunatus).

Watumiaji waliosajiliwa tu ndio wanaweza kutafsiri nakala
Ingia / Ingia
A single high-affinity binding site for adenine and related compounds was identified in the lima bean lectin (LBL) component III tetramer. This site is identical with the high affinity site for 2,6-toludinyl-naphthalenesulfonate described previously (Roberts, D. D., and Goldstein, I. J. (1982) J.
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