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Bioenergetics: a practical approach
482 source of recombinant DNA libraries. Both volumes give good practical details on how to carry out the different procedures. Cell growth and apoptosis: a practical approach. Edited by G. P. Studzinski. 268 pp. 1995. Oxford, IRL/Oxford University Press. £27.50. Apoptosis (controlled cell death), unlike necrosis, produces little or no inflammation; it can be induced by cancer therapeutic agents, and it is fundamental in the normal development of tissues and organs. This book deals with measuring parameters of cell growth; flow cytometry analysis of the cell cycle; analysis of flow cytometric DNA histograms; cell proliferative fraction in human tumors; chromosome analysis in cell culture; assessment of DNA damage in mammalian cells by DNA filter elution; morphological and biochemical criteria of apoptosis; analysis of cell death by flow cytometry; cell growth and cytotoxicity; cell synchronization as a basis for investigating control of proliferation in mammalian cells; human leukemic cells in vitro and their growth in SCID mice; senescence and immortalization of human cells; and analysis of the effects of purified growth factors on normal human fibroblasts. Little by little, we are getting to understand more about cell growth and death. Pulsed field gel electrophoresis: a practical approach. Edited by A. P. Monaco. 198 pp. 1995. Oxford, IRL/Oxford University Press. £25. Pulsed field gel electrophoresis (PFGE) has provided a reliable system for the separation of DNA fragments greater than 50 kb and has made a major impact in the analysis of prokaryotic and eukaryotic genomes. PFGE was used to construct long-range (1-10 Mb) restriction maps of mammalian chromosomal regions. Practical details are given concerning gel etectrophoresis of high-molecular-weight DNA; PFGE in physical mapping; mutation detection and diagnosis; cloning from PFGE purified genomic DNA fragments and yeast artificial chromosomes (YACs); YAC cloning using PGFE; analysis of YACs; functional analysis of mammalian genomes using YACs; PFGE in study of Haemophilus influenzae; and analysis of genomes of protozoan parasites (malaria, Leishmania, Trypanosomes).
Book Reviews Methods in protein structure analysis. Edited by M. Atassi and E. Appella. 534 pp. 1995. New York, Plenum Press. £125. It is necessary to know the structure of peptides and proteins to understand their functional groups and how they work in the body. This volume contains the papers presented at the 10th MPSA conference. The papers were grouped into 8 sections: (1) protein and peptide preparation for microsequence analysis; (2) N-terminal sequence analysis; (3) C-terminal analysis; (4) mass spectrometry; (5) new strategies for protein and peptide characterization; (6) immunological recognition, phage, and synthetic libraries; (7) analysis of protein structures of special interest (GABA receptor polypeptide; DNA-PK, p53 tumor supressor protein; human fibrinogen; rough endoplasmic membrane proteins; human leukocyte collage; apoB-100); and (8) database analysis, protein folding, and the three-dimensional structures of proteins.
Guidebook to the small GTPases. Edited by M. Zerial and L. A. Huber. 476 pp. 1995. Oxford, Sambrook & Tooze/Oxford University Press. £29.50. The superfamily of small GTPases are related to the proto-oncogene p21 Ras and are key players in controlling cell growth, differentiation, and intracellular organization. They are inactive when bound to GDP and are activated by binding to GTP. The active conformation acts as a switch that is uniquely capable of recognizing the target molecule to produce the characteristic effect. The intrinsic or catalyzed OTPase activity ensures that the switch remains active for only a fixed time. Eukaryotic cells probably use several hundred different GTPases to control processes ranging from protein synthesis to cell growth. More than 70 different small GTPases have been identified, and based on their structural and functional properties they have been grouped into 6 different families: (1) overview of the Ras superfamily; (2) the Ras subfamily; (3) the Rho subfamily; (4) the Rab subfamily; (5) the Arf and Sar subfamilies; and (6) the Ran subfamily. The 140 authors provide key information on the structure and function of the 70 small GTPases and will get you up-to-date and switched on.
Bioenergetics: a practical approach. Edited by G.C. Brown and C. E. Cooper. 224 pp. 1995. Oxford, IRL/Oxford University Press. £27.50.
Aspartic proteinases: structure, function, biology and biomedical implications. Edited by K. Takahashi. 629 pp. 1995. New York, Plenum Press. $139.
The molecular mechanisms of ion translocating proteins has aroused considerable interest. The application of new techniques such as patch clamp, NMR, and EPR have provided more information about the mechanisms and stoichiometric relationships. This book gives practical details for the measurement of oxygen, proton, and phosphate fluxes; membrane permeability and transport; mitochondrial proton motive force; reconstitution of bioenergetic proteins and the use of proteoliposomes; redox states and potentials; control and regulation in bioenergetics; patch clamp of mitochondria and proteoliposomes; 31p NMR; and isolation of photosynthetic reaction centers.
This volume contains the proceedings of the 5th International Symposium on aspartic proteinases (AP). APs have two aspartic acid residues in their active sites. There are papers on gastric APs (progastricsin, pepsinogen, pepsin); non-gastric APs (renins, cathespin E, cathepsin D. cyprosins); retroviral APs; and microbial APs. They describe X-ray structural studies; protein engineering by site A-directed mutagenesis; the design and chemical synthesis of new inhibitors; and the properties of retroviral APs, H1V, renin, Candida APs, and malarial parasite APs.
Book Reviews Methods in protein structure analysis. Edited by M. Atassi and E. Appella. 534 pp. 1995. New York, Plenum Press. £125. It is necessary to know the structure of peptides and proteins to understand their functional groups and how they work in the body. This volume contains the papers presented at the 10th MPSA conference. The papers were grouped into 8 sections: (1) protein and peptide preparation for microsequence analysis; (2) N-terminal sequence analysis; (3) C-terminal analysis; (4) mass spectrometry; (5) new strategies for protein and peptide characterization; (6) immunological recognition, phage, and synthetic libraries; (7) analysis of protein structures of special interest (GABA receptor polypeptide; DNA-PK, p53 tumor supressor protein; human fibrinogen; rough endoplasmic membrane proteins; human leukocyte collage; apoB-100); and (8) database analysis, protein folding, and the three-dimensional structures of proteins.
Guidebook to the small GTPases. Edited by M. Zerial and L. A. Huber. 476 pp. 1995. Oxford, Sambrook & Tooze/Oxford University Press. £29.50. The superfamily of small GTPases are related to the proto-oncogene p21 Ras and are key players in controlling cell growth, differentiation, and intracellular organization. They are inactive when bound to GDP and are activated by binding to GTP. The active conformation acts as a switch that is uniquely capable of recognizing the target molecule to produce the characteristic effect. The intrinsic or catalyzed OTPase activity ensures that the switch remains active for only a fixed time. Eukaryotic cells probably use several hundred different GTPases to control processes ranging from protein synthesis to cell growth. More than 70 different small GTPases have been identified, and based on their structural and functional properties they have been grouped into 6 different families: (1) overview of the Ras superfamily; (2) the Ras subfamily; (3) the Rho subfamily; (4) the Rab subfamily; (5) the Arf and Sar subfamilies; and (6) the Ran subfamily. The 140 authors provide key information on the structure and function of the 70 small GTPases and will get you up-to-date and switched on.
Bioenergetics: a practical approach. Edited by G.C. Brown and C. E. Cooper. 224 pp. 1995. Oxford, IRL/Oxford University Press. £27.50.
Aspartic proteinases: structure, function, biology and biomedical implications. Edited by K. Takahashi. 629 pp. 1995. New York, Plenum Press. $139.
The molecular mechanisms of ion translocating proteins has aroused considerable interest. The application of new techniques such as patch clamp, NMR, and EPR have provided more information about the mechanisms and stoichiometric relationships. This book gives practical details for the measurement of oxygen, proton, and phosphate fluxes; membrane permeability and transport; mitochondrial proton motive force; reconstitution of bioenergetic proteins and the use of proteoliposomes; redox states and potentials; control and regulation in bioenergetics; patch clamp of mitochondria and proteoliposomes; 31p NMR; and isolation of photosynthetic reaction centers.
This volume contains the proceedings of the 5th International Symposium on aspartic proteinases (AP). APs have two aspartic acid residues in their active sites. There are papers on gastric APs (progastricsin, pepsinogen, pepsin); non-gastric APs (renins, cathespin E, cathepsin D. cyprosins); retroviral APs; and microbial APs. They describe X-ray structural studies; protein engineering by site A-directed mutagenesis; the design and chemical synthesis of new inhibitors; and the properties of retroviral APs, H1V, renin, Candida APs, and malarial parasite APs.