scholarly journals Evaluación de la cosecha de plantas seleccionadas de henequén (Agave fourcroydes Lem) y propagadas in vitro

2018 ◽  
Vol 14 (33) ◽  
pp. 17
Author(s):  
Gerardo González ◽  
Silvia Alemán ◽  
Hilter Figueroa Saavedra ◽  
Arisdorgan Diéguez ◽  
Ramiro Herrera
Keyword(s):  
Conventional Method ◽  
Vascular Bundle ◽  
Fibre Content ◽  
Agave Fourcroydes ◽  
Productive Potential ◽  
Agricultural Yields ◽  
Production Conditions

This paper focuses on the establishment of a system of in vitro cloning of henequen, of which the behavior of these plants in production conditions is unknown. With the objective of evaluating the agricultural yields in selected henequen and plants propagated in vitro, five harvests were carried out during the years 2005 to 2009. In the five harvest, the yields in fiber (tn/ha) were higher in the vitroplantas in regards to conventionally propagated plants. The first harvest was done three years after the plantation was carried out. In all crops, line 4 statistically surpassed lines 1 and 9 in terms of the fibre content, which showed a greater productive potential. The histological characterization of these plants showed a greater number of vascular bundle and strands of fibers in the vitroplants with regard to plants multiplied by the conventional method. This, however, showed a significant correlation with more fibre content in the first.

On visions and promises — ethical aspects of in vitro meat

2019 ◽  
Vol 3 (6) ◽  
pp. 753-758
Author(s):  
Silvia Woll
Keyword(s):  
Animal Welfare ◽  
Environmental Issues ◽  
Meat Production ◽  
Ethical Aspects ◽  
Existing Problems ◽  
In Vitro Meat ◽  
Production And Consumption ◽  
Production Conditions

Innovators of in vitro meat (IVM) are convinced that this approach is the solution for problems related to current meat production and consumption, especially regarding animal welfare and environmental issues. However, the production conditions have yet to be fully clarified and there is still a lack of ethical discourses and critical debates on IVM. In consequence, discussion about the ethical justifiability and desirability of IVM remains hypothetical and we have to question those promises. This paper addresses the complex ethical aspects associated with IVM and the questions of whether, and under what conditions, the production of IVM represents an ethically justifiable solution for existing problems, especially in view of animal welfare, the environment, and society. There are particular hopes regarding the benefits that IVM could bring to animal welfare and the environment, but there are also strong doubts about their ethical benefits.

Assays for Phospholipid-Dependent Formation of Thrombin and Xa: A Potential Method for Quantifying Lupus Anticoagulant Activity

1991 ◽  
Vol 66 (04) ◽  
pp. 453-458 ◽  
Author(s):  
John T Brandt
Keyword(s):  
Specific Activity ◽  
Anticoagulant Activity ◽  
Factor Xa ◽  
Clinical Importance ◽  
Potential Method ◽  
Quantitative Expression ◽  
Increased Risk ◽  
Apparent Association

SummaryLupus anticoagulants (LAs) are antibodies which interfere with phospholipid-dependent procoagulant reactions. Their clinical importance is due to their apparent association with an increased risk of thrombo-embolic disease. To date there have been few assays for quantifying the specific activity of these antibodies in vitro and this has hampered attempts to purify and characterize these antibodies. Methods for determining phospholipid-dependent generation of thrombin and factor Xa are described. Isolated IgG fractions from 7 of 9 patients with LAs were found to reproducibly inhibit enzyme generation in these assay systems, permitting quantitative expression of inhibitor activity. Different patterns of inhibitory activity, based on the relative inhibition of thrombin and factor Xa generation, were found, further substantiating the known heterogeneity of these antibodies. These systems may prove helpful in further purification and characterization of LAs.

Characterization of the Original Christmas Disease Mutation (Cysteine 206 → Serine): From Clinical Recognition to Molecular Pathogenesis

1992 ◽  
Vol 67 (01) ◽  
pp. 063-065 ◽  
Author(s):  
Sherryl A M Taylor ◽  
Jacalyn Duffin ◽  
Cherie Cameron ◽  
Jerome Teitel ◽  
Bernadette Garvey ◽  
...  
Keyword(s):  
Nucleotide Substitution ◽  
Novel Mutation ◽  
Factor Ix ◽  
Causative Mutation ◽  
Coding Region ◽  
Body Of Knowledge ◽  
Polymerase Chain ◽  
Splice Junctions

SummaryChristmas disease was first reported as a distinct clinical entity in two manuscripts published in 1952 (1, 2). The eponym associated with this disorder, is the surname of the first patient examined in detail and reported by Biggs and colleagues in a paper describing the clinical and laboratory features of seven affected individuals (3). This patient has severe factor IX coagulant deficiency (less than 0.01 units/ml) and no detectable circulating factor IX antigen (less than 0.01 units/ml). Coding sequence and splice junctions of the factor IX gene from this patient have been amplified in vitro through the polymerase chain reaction (PCR). One nucleotide substitution was identified at nucleotide 30,070 where a guanine was replaced by a cytosine. This mutation alters the amino acid encoded at position 206 in the factor IX protein from cysteine to serine. The non conservative nature of this substitution, the absence of this change in more than 200 previously sequenced factor IX genes and the fact that the remainder of the coding region of this gene was normal, all provide strong circumstantial evidence in favour of this change being the causative mutation in this patient. The molecular characterization of this novel mutation in the index case of Christmas disease, contributes to the rapidly expanding body of knowledge pertaining to Christmas disease pathogenesis.

IN VITRO/IN SILICO CHARACTERIZATION OF ACTIVE AND PASSIVE STRESSES IN CARDIAC MUSCLE

2012 ◽  
Vol 10 (2) ◽  
pp. 171-188 ◽  
Author(s):  
Markus Boel ◽  
Oscar J. Abilez ◽  
Ahmed N Assar ◽  
Christopher K. Zarins ◽  
Ellen Kuhl
Keyword(s):  
Cardiac Muscle ◽  
In Silico ◽  
In Silico Characterization

Rapid, Refined, and Robust Method for Expression, Purification, and Characterization of Recombinant Human Amyloid-beta M1-42

2019 ◽  
Author(s):  
Priya Prakash ◽  
Travis Lantz ◽  
Krupal P. Jethava ◽  
Gaurav Chopra
Keyword(s):  
Amyloid Beta ◽  
Western Blots ◽  
Force Microscopy ◽  
E Coli ◽  
Atomic Force ◽  
Set Up ◽  
Short Time

Amyloid plaques found in the brains of Alzheimer’s disease (AD) patients primarily consists of amyloid beta 1-42 (Ab42). Commercially, Ab42 is synthetized using peptide synthesizers. We describe a robust methodology for expression of recombinant human Ab(M1-42) in Rosetta(DE3)pLysS and BL21(DE3)pLysS competent E. coli with refined and rapid analytical purification techniques. The peptide is isolated and purified from the transformed cells using an optimized set-up for reverse-phase HPLC protocol, using commonly available C18 columns, yielding high amounts of peptide (~15-20 mg per 1 L culture) in a short time. The recombinant Ab(M1-42) forms characteristic aggregates similar to synthetic Ab42 aggregates as verified by western blots and atomic force microscopy to warrant future biological use. Our rapid, refined, and robust technique to purify human Ab(M1-42) can be used to synthesize chemical probes for several downstream in vitro and in vivo assays to facilitate AD research.

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