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This is a laboratory manual for experimentalparasitologists, very nicely produced in aclear and robust A5 ring-bound format. Itwas written for postgraduate andpostdoctoral scientists and is intended toillustrate and encourage the use of a widediversity of methodological approaches byexperimental parasitologists.
There are thus ten chapters covering abroad spectrum of methods, ranging fromthe generic to the highly specialized. In thefirst category are descriptions of the methodsused in the electrophoretic analysis ofproteins (Eileen Devaney) and in electron
microscopy (Andrew Hemphill and SimonCroft), together with a selection of thebasic nucleic acid techniques (StevenHeath) and antibody-based analyticalmethods (Michael T. Rogan). Morespecialized are the chapters on methods fordetermining parasite biochemical pathways(John Barrett), and for studying helminthexcretory/secretory products (Alan Brownand colleagues), parasite proteinases(Michael J. North), helminth neurobiology(Aaron G. Maule and colleagues) and finallyfluorescent- and caged-compoundmethodology (J. Modha et al.) and lectin-
based methods for analysis of parasitesurface carbohydrates (George A. Ingram).
These are expert and enthusiasticauthors who have mined their lab booksunstintingly in compiling these chapters but this manual is much more than acollection of protocols as there are manyadditional practical tips. Each chapter alsoexplains the principles and problemsinvolved and many have extensivereference lists. This is a very useful manual,although the cover price of DM 128.00 willdeter some private buyers.
Martin TaylorImmunology Unit Department of Infectious and Tropical Diseases London School of Hygiene and Tropical MedicineKeppel StreetLondon, UK WC1E 7HT
References1 Kolodziej, A.K. and Young, R.A. (1991)
Methods Enzymol. 194, 508–5192 Piper, R.C. et al. (1995) J. Cell Biol. 128,
499–5083 Traub-Cseko, Y.M. et al. (1993) Mol. Biochem.
Parasitol. 57, 101–1164 Duboise, S.M. et al. (1994) Mol. Biochem.
Parasitol. 68, 119–1325 Shafer, K. and Braun, T. (1995) Biochem.
Biophys. Res. Commun. 207, 708–7146 Nakai, Y. et al. (1986) Intervirology 25, 30–377 Wilson, I.A. et al. (1984) Cell 37, 767–7788 Evan, G.I. et al. (1989) Mol. Cell. Biol. 5,
3610–36169 Chubet, R.G. and Brizzard, B.L. (1996)
BioTechniques 20, 136–141
Yara M. Traub-CsekoDiamar Costa-PintoOswaldo Cruz Institute, FIOCRUZ Department of Biochemistry and Molecular
Biology PO Box 926 Rio de Janeiro, RJ, Brazil
Diane McMahon-PrattYale University School of Medicine LEPH, New Haven, CT, USA
Letters
Book Reviews
42 Parasitology Today, vol. 14, no. 1, 1998
Table 1. Commercial monoclonal antibodies, their antigenic sequence, origin and manufacturer
Epitope Origin Manufacturer Ref.AU1 DTYRYI L1 capsid protein of bovine BAbCO 6
papillomavirus (BPV) Anti-HA YPYDVPDYA Influenza hemagglutinin protein Boehringer 7
[12CA5]a
Anti-c-myc EQKLISEEDL Human tumors including lung, Santa Cruz Biotechnology 8[9E10] breast and colon carcinomas
Anti-FLAG DYKDDDDK Highly charged and soluble Scientific Imaging System, 9[M2] peptide Eastman Kodak Co.
a The commercial denominations of the monoclonal antibodies are shown in square brackets.
Table 2. Western blot dataa
L. pifanoi L. pifanoi L. panamensis L. panamensis L. amazonensis L. braziliensis L. donovani L. major L. mexicanamAb ama pm am pm pm pm pm pm pmC-myc 45; 40 40 45 45 15 –a 17 – 17M2 50 50 50; 35 50; 35 38 42 40 – 36Anti-HA 45 45 45 45 nda nd nd nd ndAU1 – – – – – – – – –
a Molecular mass (kDa) of Leishmania components recognized by monoclonal antibodies specific for epitope tag. am, amastigote; pm, promastigote; ‘–’,no reaction; nd, not done.
Table 3. Immunofluorescence dataa
Leishmania pifanoi Leishmania panamensis
Amastigote Promastigote Amastigote PromastigoteAU1 2 2 2 2C-myc 1 1 1 1
dc dc dc pcAnti-HA 1 1 1 1
pc dc pc dcM2 1 1 1 1
dc dc flagellar pocket surface
a ‘2’, negative; ‘1’, positive; dc, diffuse cytoplasmic; pc, punctate cytoplasmic.
Analytical Parasitologyedited by M.T. Rogan, Springer, 1997. DM128.00 (365 pages) ISBN 3 540 58919 8