ArticleReports of biochemistry & molecular biology2019
Analysis of Methods to Improve the Solubility of Recombinant Bovine Sex Determining Region Y Protein.
Article in Reports of biochemistry & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Soluble Expression of Recombinant Human Mitsugumin 53 in Escherichia coli NiCo21(DE3).The protein journal · 2026Article
- Toward Safer Biotherapeutics: Expression and Characterization of a Humanized Chimeric L-Asparaginase inInternational journal of molecular sciences · 2025Article
- Machine learning modeling for solubility prediction of recombinant antibody fragment in four different E. coli strains.Scientific reports · 2022Article
- Cloning, expression, and in silico structural modeling of cholesterol oxidase of Acinetobacter sp. strain RAMD in E. coli.FEBS open bio · 2021Article
- Heterologous expression, purification, and refolding of SRY protein: role of L-arginine as analyzed by simulation and practical study.Molecular biology reports · 2020Article
- Goat Polyclonal Antibody Against the Sex Determining Region Y to Separate X- and Y-Chromosome Bearing Spermatozoa.Reports of biochemistry & molecular biology · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundInclusion body formation in
methodsIn this research two recombinant bovine SRY (rbSRY) sequences were analyzed; these were wildtype SRY (wtbSRY) and codon-optimized SRY (cobSRY). Their expression in various culture conditions was examined; these differences included IPTG concentrations, temperatures, and media stabilizers.
resultsIPTG and temperature significantly affected rbSRY solubility (P < 0.001). The optimum IPTG concentration and temperatures for wtbSRY and cobSRY induction were 0.3 mM at 27 and 32 °C,respectively. In addition, arginine and sorbitol concentrations significantly affected rbSRY solubility (P <0.01). Solubility of rbSRY protein was highest from the cobSRY construct in the presence 0.2 M arginine and 0.3 M sorbitol. The highest inclusion body production occurred with high glucose concentrations.
conclusionWe found that modifications in temperature and IPTG and stabilizer concentrations affected rbSRY solubility.
Indexed as
Identifiers
32274394PMC7103077W3005639175What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.