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https://www.readbyqxmd.com/read/27629861/methodological-challenges-in-developing-a-youth-questionnaire-life-health-young-people-for-comparative-studies-in-thailand-and-sweden-about-bridging-the-language-gap-between-two-non-english-speaking-countries
#1
Anchalee Thitasan, Marianne Velandia, Chularat Howharn, Elinor Brunnberg
PURPOSE: To develop a Thai questionnaire ชีวิตและสุขภาพของวัยรุ่นในประเทศไทย (TYQ) to explore girls' and boys' living conditions, lifestyles, and self-reported health with special focus on sexuality, based on a Swedish questionnaire, Liv & Hälsa ung (SYQ). Challenges in developing a youth questionnaire for comparative studies are described. DESIGN: A multistep translation, sociocultural adaptation procedure, and a mixed-method validation test were performed using English as a common language within the research group...
September 14, 2016: Journal of Transcultural Nursing: Official Journal of the Transcultural Nursing Society
https://www.readbyqxmd.com/read/10065160/expression-isolation-and-characterization-of-a-mutated-human-plasminogen-kringle-3-with-a-functional-lysine-binding-site
#2
J Bürgin, J Schaller
Each kringle of human plasminogen (HPg) except kringle 3 (K3) exhibits affinity for omega-aminocarboxylic acids. Assuming that the K3 domain contains a preformed but nonfunctional lysine binding site (LBS), Lys311 was altered by site-directed mutagenesis into Asp311 in accordance with the consensus sequence of the LBS. Cys297 involved in the interkringle disulfide bridge was mutated into Ser297 to minimize dimerization and aggregation. The mutated K3 TYQ[K3HPg/C297S/K311D]DS (r-K3mut) was expressed in Escherichia coli, isolated on an Ni2(+)-nitrilotriacetic acid-agarose column, refolded and purified on a lysine Bio-Gel column...
January 1999: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/8307012/expression-purification-and-characterization-of-the-recombinant-kringle-2-and-kringle-3-domains-of-human-plasminogen-and-analysis-of-their-binding-affinity-for-omega-aminocarboxylic-acids
#3
COMPARATIVE STUDY
D Marti, J Schaller, B Ochensberger, E E Rickli
The kringle 2 (E161T/C162S/EEE[K2HPg/C169S]TT) and the kringle 3 (TYQ[K3HPg]DS) domains of human plasminogen (HPg) were expressed in Escherichia coli in an expression vector with the phage T5 promotor/operator element N250PSN250P29 and the cDNA sequence for a hexahistidine tail to facilitate the isolation of the recombinant protein. A coagulation factor Xa (FXa)-sensitive cleavage site was introduced to remove the N-terminal histidine tag. In r-K2, mutations E161T and C162S were introduced to enhance the FXa cleavage yield and C169S to replace the cysteine residue, participating in the inter-kringle disulfide bridge between kringles 2 and 3...
January 15, 1994: European Journal of Biochemistry
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