Biomedical subjects

Guo-An Luo

Publications and source records attributed to Guo-An Luo.

21 records · Page 2Linked to original sources

PubMed2002

Establishment of an interaction model of human apolipoprotein H with lipid monolayer by capillary SDS gel electrophoresis.

Apolipoprotein H (ApoH) is a plasma glycoprotein isolated from human serum. It plays a key role in the interaction with lipids. For the first time, the concentration of ApoH adsorbed on the lipid monolayer has been determined, and was done so using capillary electrophoresis. Based on this determination, an interaction model of ApoH and lipid monolayer was constructed, and this interaction is one of nonspecific adsorption. A neutral coated capillary (50 cm x 100 microm i.d.) and a negative voltage of 15 kV were used to separate ApoH. The calibration curve of ApoH was built using a detection limit of 50 microg/mL(-1) (near to 1 microM), and the RSD of the relative migration time of ApoH was 1.4% (n = 7).

Adsorption↗

PubMed1999

Study on the quality of recombinant proteins using matrix-assisted laser desorption ionization time of flight mass spectrometry.

AIM:To study the possibility of matrix-assisted laser esorption/ionization time of flight mass spectrometry (MALDI-TOF MS) for controlling the quality of recombinant proteins.METHODS:By using MALDI-TOF MS, the molecular weights and purity of recombinant bioactive proteins were analyzed.RESULTS:The molecular weights and purity were obtained in nine recombinant bioactive proteins, including interleukin 2,tumor necrosis factor alpha, granulocyte macrophage colony stimulating factor, interferon alpha2b, interferon alpha1, erythropoietin, calmodulin and its fragment, and neuronal nitric oxide synthase were obtained. MALDI-TOF MS was also used to assay specific proteins in the mixtures and to characterize the erythropoietin tryptic digests.CONCLUSION:The results showed that MALDI-TOF MS can be employed for the effective quality control of recombinant proteins.

Journal Article↗

PubMedDate not supplied

Monitoring the unfolding and refolding of creatine kinase by capillary zone electrophoresis.

Creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2) plays a key role in the energy transport, muscle contraction, and reproduction of adenosine triphosphate (ATP). The activity of the enzyme is dependent on the correct folding of the peptide. We observed the unfolding and refolding processes of the creatine kinase of rabbit muscle, and concluded that traditional electrophoresis technology is unsuitable for the transient folding intermediates formed during protein unfolding and refolding. Capillary zone electrophoresis with diode array detection was used to monitor the unfolding and refolding of rabbit creatine kinase under different pretreatments and experimental conditions. This technique provides a simple, sensitive, and rapid approach to protein unfolding and refolding.

Animals↗