Advances in Clinical Chemistry, Vol. 47 by Gregory S. Makowski PDF

By Gregory S. Makowski

ISBN-10: 0123747961

ISBN-13: 9780123747969

Quantity forty seven within the across the world acclaimed Advances in medical Chemistry includes chapters submitted from top specialists from academia and scientific laboratory technological know-how. Authors are from a various box of medical chemistry disciplines and diagnostics starting from simple biochemical exploration to state-of-the-art microarray know-how. major specialists from academia and scientific laboratory technology quantity emphasizes novel laboratory advances with program to scientific laboratory diagnostics and functional easy technology stories

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Extra resources for Advances in Clinical Chemistry, Vol. 47

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1. Transthyretin Over 100 diVerent mutations are known to be associated with TTR amyloidosis [99]. TTR was previously known as prealbumin due to its position in front of albumin during protein electrophoresis but it is now known to be a hepatically synthesized protein which functions as a carrier of thyroxine and retinol. The Val30Met mutation is the most common and frequently presents in large foci around the world [99] (Fig. 6). In northern Sweden it is reported that in a population of 500,000, 7500 people carry the mutation although the penetrance of the disease is only 2% [100].

Martin, A. Livneh, M. R. Gallo, Biochemical subtyping of amyloid in formalin‐fixed tissue samples confirms and supplements immunohistologic data, Am. J. Clin. Pathol. 121 (6) (2004) 794–800. [53] B. Kaplan, S. Shtrasburg, M. Pras, Micropurification techniques in the analysis of amyloid proteins, J. Clin. Pathol. 56 (2) (2003) 86–90. AMYLOIDOSIS 39 [54] A. Kebbel, C. Rocken, Immunohistochemical classification of amyloid in surgical pathology revisited, Am. J. Surg. Pathol. 30 (6) (2006) 673–683.

M. Hartley, Y. Kusumoto, Y. M. Condron, A. , Amyloid beta‐protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates, J. Biol. Chem. 274 (36) (1999) 25945–25952. R. A. K. L. Lin, R. H. , Growth of beta‐amyloid(1‐40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy, Biochemistry 41 (19) (2002) 6115–6127. [20] T. A. Haller, E. Luttmann, J. Kruger, G. Fels, K. Huber, Time resolved structure analysis of growing beta‐amyloid fibers, J.

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Advances in Clinical Chemistry, Vol. 47 by Gregory S. Makowski


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