Plant biotechnology

Book Review

Plant biotechnologyS.-D. Kung and C.J. Arntzen (Eds.) Boston: Butterworths, 1989. xxi + 423 pages. £60.00. ISBN 0-409-90068-0     

Seed dormancy and germination (tertiary level biology)

Book review

Seed dormancy and germination (tertiary level biology)J W Bradbeer, Glasgow: Blackie &; Son 1988. x + 146 pages. £23.00 hardback; £10.95 paperback. ISBN 0-216 91635-6; ISBN 0-216-91636-4 PbK     

Improving vegetatively propagated crops

Book reviews

Improving vegetatively propagated cropsA.J. Abbott and R.K. Atkin (Eds.), London: Academic Press, 1987. xvii + 416 pages. £37.00. 0-12-041410-4     

Aspects of floral development

Book Review

Aspects of floral developmentP. Leins, S.C. Tucker and P.K. Endress (Eds.), Berlin: J. Cramer, 1988. vii + 239 pages. ISBN 3-443-50011-0     

Plant membranes: Structure,assembly and function

Book Review

Plant membranes: Structure, assembly and functionJ.L. Harwood and T.J. Walton (Eds.), London: The Biochemical Society, 1988, 251 pages. £25. ISBN 0-904498-23-9     

Badger Badger. T. J. Roper. HarperCollins Publishers. London. 2010, 388 pp. ISBN 978-0-00-733977-8

Book Review

Badger Badger. T. J. Roper. HarperCollins Publishers. London. 2010, 388 pp. ISBN 978-0-00-733977-8     

Molecular biology of photosynthesis

Book reviews

Molecular biology of photosynthesisGovindjee, H.J. Bohnert, W. Bottomley, D.A. Bryant, J.E. Mullet, W.L. Ogren, H. Pakrasi, and C.R. Somerville (Eds.), Dordrecht: Kluwer Academic Publishers, 1989. xxvii + 815 pages. £130.00. ISBN 0-7923-0097-1     

Structure and functional aspects of transport in roots

Book reviews

Structure and functional aspects of transport in rootsB.C. Loughman. O. Gasparikova and J. Kolek (Eds.) (Developments in plant and soil sciences, volume 36). Dordrecht: Kluwer Academic Publishers 1989. xii + 274 pages. £49.00. ISBN 0-7923-0060-2.     

Molecular and genetic aspects of nitrate assimilation

Book Review

Molecular and genetic aspects of nitrate assimilationJ.L. Wray and J.R. Kinghorn (Eds.), Oxford, New York, Tokyo: Oxford Science Publications, 1989. xv + 410 pages. £45.00. ISBN 0-19-857696-X     

Progress in theoretical vegetation science

Book Review

Progress in theoretical vegetation scienceG. Grabhett, L. Mucina, M.B. Dale and C.J.F. ter Braak (Eds.), Vol 83. Dordrecht: Kluwer Academic Publishers, 1990, 276 pages, £95.00. ISBN 0-7923-0507-1     

Selective cytotoxicity of intense nanosecond-duration electric pulses in mammalian cells

Background

Nanosecond electric pulses (EP) disrupt cell membrane and organelles and cause cell death in a manner different from the conventional irreversible electroporation. We explored the cytotoxic effect of 10-ns EP (quantitation, mechanisms, efficiency, and specificity) in comparison with 300-ns, 1.8- and 9-μs EP.

Methods

Effects in Jurkat and U937 cells were characterized by survival assays, DNA electrophoresis and flow cytometry.

Results

10-ns EP caused apoptotic or necrotic death within 2–20 h. Survival (S, %) followed the absorbed dose (D, J/g) as: S = αD^(−K), where coefficients K and α determined the slope and the “shoulder” of the survival curve. K was similar in all groups, whereas α was cell type- and pulse duration-dependent. Long pulses caused immediate propidium uptake and phosphatidylserine (PS) externalization, whereas 10-ns pulses caused PS externalization only.

Conclusions

1.8- and 9-μs EP cause cell death efficiently and indiscriminately (LD₅₀ 1–3 J/g in both cell lines); 10-ns EP are less efficient, but very selective (LD₅₀ 50–80 J/g for Jurkat and 400–500 J/g for U937); 300-ns EP show intermediate effects. Shorter EP open propidium-impermeable, small membrane pores (”nanopores”), triggering different cell death mechanisms.

General significance

Nanosecond EP can selectively target certain cells in medical applications like tumor ablation.     

Biotechnology in agricultural chemistry

Book Review

Biotechnology in agricultural chemistryH.M. LeBaron, R.O. Mumma, R.C. Honeycutt and J.H. Duesing (Eds.), ACS Symposium Series 334, Washington, DC. American Chemical Society, 1987. xxii + 367 pages. US $77.95 ISBN 0-8412-1010-5     

Influence of the xyloadenosine analogue of 2′,5′-oligoriboadenylate on poly(A)-specific, 2′,5′-oligoriboadenylate degrading 2′,3′-exoribonuclease and further enzymes involved in poly(A)(+)mRNA metabolism

The homogeneous poly(A)-specific 2,3-exoribonuclease from calf thymus gland, which cleaves both 3,5-and 2,5-linked oligoriboadenylates, does not degrade (xyloA2'p)₂ xyloA, the xylofuranosyladenosine analogue of the 2-5A core. This oligonucleotide, which is supposed to enter intact cells rapidly, was found to possess an increased stability and an enhanced antiherpesvirus activity compared to the natural (A2'p)₂A (Eppstein, D. A., Barnett, J. W., Marsh, Y. V., Gosselin, G. and Imbach, J.-L. (1983) Nature 302, 723–724). The poly(A) anabolic enzyme, poly(A) polymerase (Mn²⁺-dependent), from the same source, which is initiated by (A3'p)₂A and its higher oligomers, does not accept 2–5A core and its xyloadenosine analogue as primer. Both oligonucleotides exert no influence on endoribonuclease IV and on the integrity of the poly(A)-ribonucleoprotein complex.Abbreviations 2-5A ppp(A2'p)_nA(n2). 5-triphospho-oligo [(2–5)adenylyl]adenosine - 2-5A core (A2'p)₂A, adenylyl(2–5) adenylyl(2–5)adenosine - xyto 2-tA core (xyloA2'p)₂ xyloA, xyloadenylyl(2–5)xyloadenylyl(2–5)xyloadenosine The other abbreviations are according to the recommendations of the Commission on Biochemical Nomenclature, see Europ. J. Biochem.15 (1970) 203–208.     

Plant analysis — as a guide to the nutrient requirements of temperate and tropical crops

Book review

Plant analysis — as a guide to the nutrient requirements of temperate and tropical cropsP. Martin-Prevel, J. Gagnard and P. Gautier (Eds.), [translated from the French by M.R.J. Holmes]. New York: Lavoisier Publishing Inc., 1987. xx + 722 pages. US$112. ISBN 2-85206-364-6     

La fuerza de prensión manual: ¿puede ser un factor pronóstico de mortalidad en cuidados paliativos?

Objective

To determine whether hand grip strength (HGS) is a prognostic factor for mortality in a palliative care unit (PCU), using two variables: A1: The HP on admission; A2: The progression of the HGS in the first 12 days of admission.

Material and methods

A prospective, observational and comparative study of patients with advanced cancer admitted consecutively over a 4 month period into a PCU. A series of 4 determinations of HGS were made using a JAMAR^® 5030J1 dynamometer. A total of 78 patients fulfilled the inclusion criteria, of which 61 (78.2%) agreed to take part.

Results

Objective A1: Of the 61 enrolled patients, the survivors (n = 25) differed by -1.8 (Standard Deviation (SD) 0.8) from the reference values for age and gender, and for those that died (n = 36) it was -1.9 (1.1) (P = .6). A survival analysis was performed with this sample. The sample was subdivided into those who were > -2 SD (n = 34) and those < -2 SD (n = 27) (P = .3). Those patients who managed 4 determinations (n = 49) were included in objective A2. At discharge there were 26 deaths and 23 alive. There were no statistically significant differences between the determinations. Only the comparison between the difference between the 4th and 1st determination in the two groups showed a significant result (P = .01).

Conclusions

The HGS measured at admission, as well as in the first 12 days, was not a prognostic factor for mortality in the sample studied.     

Developmental control of the expression of two ten-sugar branched chain fucolipids in rat small intestine

Two branched decaglycosylceramides, apparently identical to those identified in the small intestine of adult rats [Breimer ME, Falk K-E, Hansson GC, Karlsson K-A (1982) J Biol Chem 257:50–59], were absent during the three weeks following birth. They appeared abruptly at around 21 days. After their appearance, their tissue concentration and their base composition did not change during development. Their fatty acids were non-hydroxylated and the percentage of C₂₂–C₂₄ fatty acids, which was low at 24 days, increased and reached 48.6% by 27 days.Nomenclature Gal1-4Gal1-4GlcCer Globotriaosylceramide (GbOse₃Cer) - Il³NeuAc-LacCer M_M3-ganglioside - GalNAc1-3Gal1-4Gal1-4GlcCer globoside (globotetraosylceramide, GbOse₄Cer)     

A simple method to quantitatively measure polypeptide JHNHα coupling constants from TOCSY or NOESY spectra

A simple linear relationship between the J coupling constant and the linewidth (_1/2) of in-phase NMR peaks has been identified. This relationship permits the rapid and accurate determination of polypeptide J coupling constants from a simple inspection of amide cross peaks in homonuclear ¹H TOCSY or ¹H NOESY spectra. By using the appropriate set of processing parameters we show that J = 0.5(_1/2) – MW/5000 + 1.8 for TOCSY spectra and J = 0.6(_1/2) – MW/5000 – 0.9 for NOESY spectra, where _1/2 is the half-height linewidth in Hz and MW is the molecular weight of the protein in Da. The simplicity of this relationship, combined with the ease with which _1/2 measurements can be made, means that J coupling constants can now be rapidly determined (up to 100 measurements in less than 30 min) without the need for any complex curve-fitting algorithms. Tests on 11 different polypeptides involving more than 650 separate J measurements have shown that this method yields coupling constants with an rmsd error (relative to X-ray data) of less than 0.9 Hz. Furthermore, the correlation coefficient between the predicted NMR coupling constants and those derived from high-resolution X-ray crystal structures is typically better than 0.89. These simple linear relationships have been found to be valid for peptides as small as 1 kDa to proteins as large as 20 kDa. Despite the method's simplicity, these results are comparable to the accuracy and precision of the best techniques published to date.     

Intact and N- or C-terminal end truncated AQP0 function as open water channels and cell-to-cell adhesion proteins: End truncation could be a prelude for adjusting the refractive index of the lens to prevent spherical aberration

Background

Investigate the impact of natural N- or C-terminal post-translational truncations of lens mature fiber cell Aquaporin 0 (AQP0) on water permeability (Pw) and cell-to-cell adhesion (CTCA) functions.

Methods

The following deletions/truncations were created by site-directed mutagenesis (designations in parentheses): Amino acid residues (AA) 2–6 (AQP0-N-del-2-6), AA235–263 (AQP0-1-234), AA239–263 (AQP0-1-238), AA244–263 (AQP0-1-243), AA247–263 (AQP0-1-246), AA250–263 (AQP0-1-249) and AA260–263 (AQP0-1-259). Protein expression was studied using immunostaining, fluorescent tags and organelle-specific markers. Pw was tested by expressing the respective complementary ribonucleic acid (cRNA) in Xenopus oocytes and conducting osmotic swelling assay. CTCA was assessed by transfecting intact or mutant AQP0 into adhesion-deficient L-cells and performing cell aggregation and adhesion assays.

Results

AQP0-1-234 and AQP0-1-238 did not traffic to the plasma membrane. Trafficking of AQP0-N-del-2-6 and AQP0-1-243 was reduced causing decreased membrane Pw and CTCA. AQP0-1-246, AQP0-1-249 and AQP0-1-259 mutants trafficked properly and functioned normally. Pw and CTCA functions of the mutants were directly proportional to the respective amount of AQP0 expressed at the plasma membrane and remained comparable to those of intact AQP0 (AQP0-1-263).

Conclusions

Post-translational truncation of N- or C-terminal end amino acids does not alter the basal water permeability of AQP0 or its adhesive functions. AQP0 may play a role in adjusting the refractive index to prevent spherical aberration in the constantly growing lens.

General significance

Similar studies can be extended to other lens proteins which undergo post-translational truncations to find out how they assist the lens to maintain transparency and homeostasis for proper focusing of objects on to the retina.     

Effect of road transport for up to 24 hours followed by twenty-four hour recovery on live weight and physiological responses of bulls

Background

The transport of livestock can have major implications for their welfare, and there is strong public interest and scientific endeavour aimed at ensuring that the welfare of transported animals is optimal. The objective of the study was to investigate the effect of transport on live weight, physiological and haematological responses of bulls after road transport of 0, 6, 9, 12, 18 and 24 hours (h). Seventy-two Charolais bulls (mean weight (s.d.) 367 (35) kg), naïve to transport, were randomly assigned to one of six journey (J) times of 0 h, 6 h, 9 h, 12 h, 18 h and 24 h transport (n = 12 animals/treatment) at a stocking density of 1.02 m²/bull. Blood samples were collected by jugular venipuncture before transport (-0.25 h), immediately after (0 h) and at 1 h, 2 h, 4 h, 6 h, 8 h, 12 h and 24 h relative to time 0 h. The bulls were weighed before transport (- 24 h and - 0.25 h), immediately after (0 h), and at 4 h, 12 h and 24 h relative to time 0 h. Control animals were blood sampled before assignment (-0.25 h) to novel pens, after (24 h), and at 1 h, 2 h, 4 h, 6 h, 8 h, 12 h and 24 h relative to the 24 h sampling time point.

Results

Bulls travelling for 6 h (280 km), 9 h (435 km), 12 h (582 km), 18 h (902 km) and 24 h (1192 km) lost 4.7, 4.5, 5.7 (P < 0.05), 6.6 (P < 0.05) and 7.5 (P < 0.05) percentage (%) live weight compared with baseline. Live weight re-gained to pre-transport levels during the 24 h recovery period. Lymphocyte percentages were lower (P < 0.05) and neutrophil percentages were greater (P < 0.05) in all animals. Blood protein, glucose and NEFA concentrations and creatine kinase activity were greater (P < 0.05) in the bulls following transport and returned to baseline within 24 h.

Conclusions

Under the conditions of the present study, transport of bulls on journeys by road, ranging from 6 h (280 km) to 24 h (1192 km) duration, affected live weight, haematological and physiological measurements of metabolism and inflammation. Our findings showed that live weight and some physiological and haematological responses of bulls returned to pre-transport levels within 24 h with animals having had access to feed and water.