scholarly journals First data on growth and nucleic acid and protein content of field-captured Mediterranean bluefin (Thunnus thynnus) and albacore (Thunnus alalunga) tuna larvae: a comparative study

2006 ◽  
Vol 70 (S2) ◽  
pp. 67-78 ◽  
Author(s):  
Alberto García ◽  
Dolores Cortés ◽  
Teodoro Ramírez ◽  
Rafika Fehri-Bedoui ◽  
Francisco Alemany ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Comparative Study ◽  
Protein Content ◽  
Thunnus Thynnus ◽  
Thunnus Alalunga

Comparative Study of Size, Total Protein, Fibrinogen and 5-HT Content of Human and Canine Platelet Density Subpopulations

1986 ◽  
Vol 56 (03) ◽  
pp. 288-292 ◽  
Author(s):  
Diego Mezzano ◽  
Eduardo Aranda ◽  
Arnaldo Foradori
Keyword(s):  
Comparative Study ◽  
Protein Content ◽  
Cell Density ◽  
Total Protein ◽  
Unit Volume ◽  
Low Density ◽  
Dense Bodies ◽  
Artifactual Changes ◽  
Platelet Release ◽  
The Difference

SummaryThe size, total protein, fibrinogen and 5-HT content were evaluated in density subpopulations of human and canine platelets fractionated in linear arabinogalactan gradients. The methodology was assessed to ascertain that platelet separation was by density and to discard artifactual changes and platelet release during the procedure. EDTA or PGEi increased the size of human PRP-platelets, but not of dog platelets. In humans, high density (HD) platelets were 1.26 times larger and contained 1.88 times more fibrinogen, 2.23 times more 5-HT and 1.37 times more protein than low density (LD) platelets; in dogs, these density cohorts did not differ in protein content, but LD platelets were 1.29 times larger and had 1.33 times more fibrinogen and 5-HT than HD platelets. These findings suggest that cell density is mostly dependent on the protein content per unit volume of platelets (and not on dense bodies). The differences in fibrinogen and 5-HT content between HD and LD cohorts in humans and dogs may be related to platelet age. The difference in volume between HD and LD platelets in dogs is of uncertain interpretation.

Nucleic Acid, Protein Content, and Growth of Larval Fish Sublethally Exposed to Various Toxicants

1984 ◽  
Vol 41 (1) ◽  
pp. 141-150 ◽  
Author(s):  
Mace G. Barron ◽  
Ira R. Adelman
Keyword(s):  
Nucleic Acid ◽  
Protein Content ◽  
Larval Fish ◽  
Life Stage ◽  
Pimephales Promelas ◽  
Early Life Stage ◽  
Toxicant Exposure ◽  
Growth Measurement ◽  
Log Linear ◽  
Macromolecular Content

Larval fathead minnows (Pimephales promelas) were exposed for 96 h to several concentrations of benzophenone, ethyl acetate, hexavalent chromium, hydrogen cyanide, or p-cresol. The range of "safe" concentrations determined from 96-h macromolecular content (RNA, DNA, and protein) and growth was within or very near the range of "safe" concentrations determined by concomitant longer term exposure (28- to 32-d early life stage toxicity test). RNA, DNA, and protein content per larva and RNA/DNA ratio were sensitive to toxicant stress and followed a log-linear dose response. Larval RNA content appeared to be the 96-h measurement most responsive to toxicant exposure. A disruption of nucleic acid and protein metabolism apparently occurred within 96 h of sublethal toxicant exposure and resulted in (1) decreased rates of mitosis, (2) reduced protein synthesis, and (3) reduced growth. Measurement of growth and macromolecular content after a 96-h larval exposure provided a physiologically relevant measurement of toxicity that was predictive of longer term sublethal toxicity.

A comparative study of the protein content of some helminths and the suitability of assay methods

1991 ◽  
Vol 65 (1) ◽  
pp. 62-66
Author(s):  
S. M. A. Abidi ◽  
W. A. Nizami
Keyword(s):  
Comparative Study ◽  
Protein Content ◽  
Total Protein ◽  
Total Protein Content ◽  
Brilliant Blue G ◽  
Coomassie Brilliant Blue ◽  
Tissue Homogenates ◽  
Assay Methods ◽  
Phenol Reagent ◽  
Coomassie Brilliant

ABSTRACTThe protein content of fresh homogenates and their corresponding TCA precipitated fractions of 10 different species of helminths was estimated by the methods of Lowry et al. and Spector using the Folin phenol reagent and Coomassie brilliant blue G-250 respectively. The former method gives exaggerated values as compared to the latter method. The parasite phenols, phenolic proteins and catecholamines could be responsible for interference in the Lowry's procedure. The TCA non-precipitable moieties also give colour only with the Folin phenol assay. The pronounced intra-specific differences in the total protein content of helminths reflect their metabolic variations and adaptations. Habitat does not appear to influence the protein content of parasites, however, the effect of host variation was evident in the pouched amphistome G. crumenifer. It is concluded that the dye binding method gives more consistent results and it can be conveniently applied to crude tissue homogenates of helminths.

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