Aim To develop a rapid and inexpensive method for purification of human albumin, a method of immunomagnetic microspheres (IMMS) based on enzyme-linked immunosorbent assay (ELISA)for the purification of human albumin from human serum. Methods Polystyrene magnetic microspheres with carboxyl groups as carriers were prepared, and then the carboxyl groups on the surface of the microspheres were activated by ethylcarbodiimide (EDC). Finally rabbit anti-human serum albumin (HSA) antibodies were covalently bound to it and the complex can specifically capture HSA. After the procedure of capturing HSA, through taking rabbit anti-human albumin protein antibodies as a capture antibody, and goat anti-human albumin protein antibodies as a detection antibody, an ELISA on IMMS was developed, which can determine the recovery yield of HSA from the human serum. Results The result of the experiment was that the recovery of human albumin with IMMS was (86 ± 4) % , and IMMS were reused for two other purifying cycles, the results of which were (69.0 ± 0.6) % and (40.8 ± 0.8) % , and the purity of the product was about 90%. Conclusion The results above prove that the immunomagnetic purifiying strategy was shown to be efficient and offers an new thought for a large scale production of highpurity HSA.

OBJECTIVE: To observe the CT imaging features of anatomic structure related to endoscopic axilla approach for surgery of the frontal recess and frontal sinus. METHOD: Thirty patients without a history of frontal sinus disease were undergone 16 line high speed spiral computed tomography. The computed tomographic images were analyzed to measure the related structures. RESULT: The vertical distance from the front attachment point of the middle turbinate to the skull base was 13.88 +/- 2.59 mm. The horizontal distance from the top point of the axilla of the middle turbinate to the anterior wall of the frontal sinus outflow tract was 5.77 +/- 12.32 mm, to the anterior wall of the nasal cavity was 13.67 +/- 12.54 mm, to the lamina papyracea or lacrimal sac was 5.89 +/- 1.69 mm. CONCLUSION Sixteen line high speed spiral computed tomography is helpful to endoscopic axilla approach for surgery of the frontal recess and frontal sinus.
Adult ; Aged ; Aged, 80 and over ; Endoscopy ; methods ; Female ; Frontal Sinus ; diagnostic imaging ; surgery ; Humans ; Imaging, Three-Dimensional ; Male ; Middle Aged ; Tomography, Spiral Computed ; Turbinates ; diagnostic imaging ; surgery ; Young Adult

The corona-like spikes or peplomers on the surface of the virion under electronic microscope are the most striking features of coronaviruses. The S (spike) protein is the largest structural protein, with 1,255 amino acids, in the viral genome. Its structure can be divided into three regions: a long N-terminal region in the exterior, a characteristic transmembrane (TM) region, and a short C-terminus in the interior of a virion. We detected fifteen substitutions of nucleotides by comparisons with the seventeen published SARS-CoV genome sequences, eight (53.3%) of which are non-synonymous mutations leading to amino acid alternations with predicted physiochemical changes. The possible antigenic determinants of the S protein are predicted, and the result is confirmed by ELISA (enzyme-linked immunosorbent assay) with synthesized peptides. Another profound finding is that three disulfide bonds are defined at the C-terminus with the N-terminus of the E (envelope) protein, based on the typical sequence and positions, thus establishing the structural connection with these two important structural proteins, if confirmed. Phylogenetic analysis reveals several conserved regions that might be potent drug targets.
Amino Acid Sequence ; Antigens, Viral ; immunology ; Base Composition ; Computational Biology ; Enzyme-Linked Immunosorbent Assay ; Membrane Glycoproteins ; genetics ; Molecular Sequence Data ; Mutation ; genetics ; Phylogeny ; Protein Structure, Tertiary ; SARS Virus ; genetics ; immunology ; Sequence Analysis, DNA ; Sequence Homology ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; genetics ; metabolism