ABSTRACT
Introduction: Single-portal endoscopic carpal tunnel release using modified Agee technique is widely used in Vietnam. Yet information on the anatomy of the target space of Vietnamese people regarding this technique is scarce. We aimed to characterise the anatomical landmarks and variations of the carpal tunnel to propose a safer surgery. Materials and methods: All twenty hands of ten fresh frozen, unembalmed cadavers of Vietnamese adults were included. Dissection was performed after the vertical line, Kaplan's cardinal line and the distal wrist crease were drawn. The transverse carpal ligament (TCL), ulnar neurovascular bundle and superficial palmar arch were exposed. Measurements were made using Mitutoyo calliper. The variants of the median nerve and in the course of the thenar motor branch were recorded. Results: The median distances from the TCL distal margin to the distal wrist crease and superficial palmar arch were 31.2mm and 12.7mm, respectively. The ulnar neurovascular bundle was located 5.7mm and 4.4mm ulnar to the vertical line at the level of the TCL proximal margin and at the level of the TCL distal margin, respectively. The thenar motor branch of the median nerve was extra-ligamentous in 19 hands and preligamentous in 1 hand. Conclusion: If endoscopic portal is made along the distal wrist crease, blade assembly should not be inserted beyond the 35mm mark on its scale. Instruments should be aimed toward the radial border of the patient's ring finger. Surgeons should be aware of the preligamentous course of the thenar motor branch although this variant type is rare.
ABSTRACT
A novel fusion protein designed to facilitate protein purification was expressed in Escherichia coli and purified separately by two different chromatography methods. L-Asparaginase from Erwinia chrysanthemi is fused to the N-terminus of a model peptide, alpha-human atrial natriuretic peptide (alpha-hANP). L-Asparaginase was chosen because of its selective affinity for L-asparagine and because of its unusually high isoelectric point(8.6). A gene construction without the L-asparaginase native signal sequence caused expression at a level of 8% of total cell protein, while gene construction with the native signal sequence resulted in over five time less expression. The hybrid protein expressed without the signal sequence was purified from clarified cell lysate byeither L-asparagine affinity chromatography or cation exchange chromatography. After digestion of the fusion protein with factor Xa protease, a peptide with a molecular weight corresponding to the theoretical molecular weight of alpha-hANP was observed by coupled HPLC/mass spectrometry. (c) 1995 John Wiley & Sons Inc.
ABSTRACT
A fusion protein that contains human atrial natriuretic peptide (ANP) at its carboxy terminus has been genetically engineered with the objective of being able to produce the peptide in a process with a relatively simple purification procedure. The fusion protein also includes a (His)6 metal affinity binding site at the amino terminus, followed by Escherichia coli thioredoxin, a factor Xa protease recognition site, and ANP. With induction of the tac promoter at 30 degrees C, the expression level of the fusion protein was high (10% of total cell protein as measured by densitometry) and it was almost completely (92%) expressed as a soluble protein in the cytoplasm. A step gradient elution with imidazole of a column of Ni2+ chelated to iminodiacetic acid-agarose saturated with proteins in crude cell extract gave a very nearly pure fusion protein. After digestion of the purified fusion protein with factor Xa protease, ANP of exactly the correct size (to within 2 Da) was observed by coupled HPLC/mass spectrometry.
