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Biology subjects

Wang, Z. G.

Publications and source records attributed to Wang, Z. G..

2 recordsLinked to original sources

Research on the Estimation Model of Seedling Sowing Period Based on Different Altitude

The selection of sowing date is a key link in tobacco planting, and an appropriate sowing date can affect the survival rate and agronomic traits of tobacco plants. This study collected data on tobacco seedlings during the sowing and transplanting periods in the southwestern region of China, combined with altitude gradient data of the planting area. Time series analysis was used to construct a tobacco seedling sowing period estimation model and establish an application platform. The model was validated by comparing the survival rate of transplanting. The results indicate that the proposed LSTM model has an R2 of 0.893, a MAE of 1.796, an RSME of 2.221, and a validation model accuracy of 93.3%. The research results provide scientific sowing time basis for tobacco growers in different altitude regions, and results provide scientific sowing time basis for tobacco growers in different altitude regions, and offer suggestions for optimizing tobacco planting management and promoting the sustainable development of the tobacco industry.

ecology↗

Co-expression of recombinant human collagen α1(III) chain with viral prolyl 4-Hydroxylase in P. pastoris GS115

Prolyl 4-hydroxylase (P4H) is essential to maintain the stable triple-helix structure and function of human collagen 1([SHcy]) chain (COL3A1). To obtain hydroxylated human COL3A1, the human COL3A1 and the viral P4H A085R were co-expressed in P. pastoris GS115. The sequence of human COL3A1 without N-terminal and C-terminal was selected for expression. Colony PCR analysis and sequencing after transfection showed that the target gene had inserted successfully. Real-time quantitative PCR (RT-qPCR) indicated that human COL3A1 and P4H were expressed at the mRNA levels. SDS-PAGE and Western blotting analysis of supernatant from the recombinant methylotrophic yest culture showed that recombinant human COL3A1 (rhCOL3A1) was secreted into the culture medium with an apparent molecular mass of approximately 130 kDa. It was noted that the rhCOL3A1 expession quantity was higest at 120 h of induction. Furthermore, mass spectrometry analysis demonstrated that the rhCOL3A1 was expressed successfully. His-tagged rhCOL3A1 protein was purified by Ni-affinity column.

biochemistry↗