The finger-print sweat test

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Basic Neurology. Ed. by J. Gilroy and P. L. Holliday. Pp. vii + 373. Illustrated. R27,90. London: Macmillan. 1982.The Pathology of the Heart. By E. G. J. Olsen. Pp. ix + 402. Illustrated. R91,85. London: Macmillan. 1982.Profile of Disease and Health Care in South Africa. By H. C. J. van Rensburg and A. Mans. Pp. xvii + 319. R29,50. Pretoria: Academica Press. 1982.Principles of Ambulatory Medicine. Ed. by L. R. Barker, J. R. Burton and P. D. Zieve. Pp. xiii + 1127. Illustrated. R78,-. Baltimore, Maryland: Williams & Wilkins. 1982.Topical Reviews in Accident Surgery, vol. 2. Ed. by N. Tubbs and P. S. London. Pp. ix +258. Illustrated. £18,50. London: Wright PSG.1982.Early Care of the Injured Patient. 3rd ed. Ed. by A. J. Wait, L. F. Peltier, B. A. Pruitt jun, D. D. Trunkey and R. F. Wilson. Pp. xv + 413. Illustrated. Philadelphia: W. B. Saunders. 1982.Current Pediatric Therapy. 10th ed. By S. S. Gellis and B. M. Kagan. Pp. xxxviii + 776. R94,25. Philadelphia: W. B. Saunders. 1982.Selected Techniques in Interventional Radiology,vol. 19 (Saunders Monographs in Clinical Radiology). By S. Kadir, S. L. Kaufman, K. H. Barth and R. 1. White jun. Pp. xi +216. Illustrated. R76,75. Philadelphia: W. B. Saunders. 1982.Clinical Topics in Internal Medicine. Ed. by G. M. Tisi and H. M. Ranney. Pp. xii 173. Illustrated. Baltimore, Maryland: Williams & Wilkins. 1982.Recognizable Patterns of Human Malformation: Genetic Embryologic and Clinical Aspects (Major Problems in Clinical Pediatrics, vo!. vii). 3rd ed. By W. David and M. D. Smith. Pp. xvii + 653. Illustrated. R78,55. Philadelphia: W. B. Saunders. 1982.The Patient and the Plastic Surgeon. By R. M. Goldwyn. Pp. xiii + 255. Boston: Little, Brown. 1981.The Aging Lumbar Spine. By S. W. Wiesel, P. Bernini and R. H. Rothman. Pp. 257. Illustrated. R69,55. Philadelphia: W. B. Saunders. 1982.Postoperative Complications of Intracranial Neurological Surgery. By N. H. Horwitz and H. V. Rizzoli. Pp. xi + 472. Illustrated. Baltimore: Williams & Wilkins. 1982.Current Topics in Inflammation and Infection (International Academy of Pathology Monograph). Ed. by G. Majno, R. S. Cotran and . Kaufman. Pp. xi + 242. Illustrated. Baltimore, Maryland: Williams & Wilkins. 1982.Radiology of the Ear, Nose and Throat. By G. E. Valvassori, G. D. Porter, W. N. Hanafee, B. L. Carter and R. A. Buckingham. Pp. viii + 342. Illustrated. RI94,30. Philadelphia: \Y/. B. Saunders. 1982.Neuropathology ofParasitic Infections. By W. J. Brown and M. Voge. Pp. 240. Illustrated. RI5,-. Oxford: Oxford Medical Publishers. 1982.Herzkrankheiten: Pathophysiologie, Diagoostik, Therapie. 2nd ed. By H. Roskamm and H. Reindel!. Pp. xxxiii + 1543. Illustrated. DM 278,-. Berlin: Springer-Verlag. 1982.Review ofSpeech, Language and Hearing, vols I, 2and 3. By N. J. Lass, L. V. McReynolds, J. L. Northern and D. E. Yoder. Illustrated. R36,20 each. Philadelphia: W. B. Saunders. 1982

Fractionation of follicle stimulating hormone charge isoforms in their native form by preparative electrophoresis technology

Complex glycoprotein biopharmaceuticals, such as follicle stimulating hormone (FSH), erythropoietin and tissue plasminogen activator consist of a range of charge isoforms due to the extent of sialic acid capping of the glycoprotein glycans. Sialic acid occupies the terminal position on the oligosaccharide chain, masking the penultimate sugar residue, galactose from recognition and uptake by the hepatocyte asialoglycoprotein receptor. It is therefore well established that the more acidic charge isoforms of glycoprotein biopharmaceuticals have higher in vivo potencies than those of less acidic isoforms due to their longer serum half-life. Current strategies for manipulating glycoprotein charge isoform profile involve cell engineering or altering bioprocesss parameters to optimise expression of more acidic or basic isoforms, rather than downstream separation of isoforms. A method for the purification of a discrete range of bioactive recombinant human FSH (rhFSH) charge isoforms based on Gradiflow(TM) preparative electrophoresis technology is described. Gradiflow(TM) electrophoresis is scaleable, and incorporation into glycoprotein biopharmaceutical production bioprocesses as a potential final step facilitates the production of biopharmaceutical preparations of improved in vivo potency. (C) 2005 Elsevier B.V. All rights reserved

Purification of recombinant human growth hormone from CHO cell culture supernatant by Gradiflow preparative electrophoresis technology

Purification of recombinant human growth hormone (rhGH) from Chinese hamster ovary (CHO) cell culture supernatant by Gradiflow large-scale electrophoresis is described. Production of rhGH in CHO cells is an alternative to production in Escherichia coli, with the advantage that rhGH is secreted into protein-free production media, facilitating a more simple purification and avoiding resolubilization of inclusion bodies and protein refolding. As an alternative to conventional chromatography, rhGH was purified in a one-step procedure using Gradiflow technology. Clarified culture supernatant containing rhGH was passed through a Gradifiow BF200 and separations were performed over 60 min using three different buffers of varying pH. Using a 50 mM Tris/ Hepes buffer at pH 7.5 together with a 50 kDa separation membrane, rhGH was purified to approximately 98% purity with a yield of 90%. This study demonstrates the ability of Gradiflow preparative electrophoresis technology to purify rhGH from mammalian cell culture supernatant in a one-step process with high purity and yield. As the Gradiflow is directly scalable, this study also illustrates the potential for the inclusion of the Gradiflow into bioprocesses for the production of clinical grade rhGH and other therapeutic proteins.9 page(s