Changes in the protein concentration and volume of the haemolymph in relation to yolk deposition, ovariectomy, allatectomy, and cautery of the median neurosecretory cells in Melanoplus sanguinipes

1977 ◽  
Vol 55 (1) ◽  
pp. 97-103 ◽  
Author(s):  
R. H. Elliott ◽  
C. Gillott
Keyword(s):  
Protein Synthesis ◽  
Total Protein ◽  
Protein Concentration ◽  
Neurosecretory Cells ◽  
Corpora Allata ◽  
Total Protein Content ◽  
Concentration Increase ◽  
Protein Levels ◽  
Low Protein ◽  
Median Neurosecretory Cells

The protein concentration and volume of the haemolymph may change with no apparent relation to one another in normal, ovariectomized, allatectomized, and median-neurosecretorycell-cauterized (mNSC-cauterized) females. Therefore, protein levels in the haemolymph are more meaningfully expressed in terms of the total protein content. In normal females, fluctuations in the haemolymph volume tend to parallel changes in the protein concentration during the first and subsequent gonotrophic periods. However, significantly less protein accumulates during the latter periods. The suggestion that these fluctuations partly reflect changes in the vitellogenic requirements of the oocytes is supported by the finding that both the volume and protein concentration increase significantly after ovariectomy.Allatectomy or mNSC cautery prevents the normal accumulation of protein in the haemolymph. In allatectomized females, the slight increase in protein concentration is accompanied by a decline in haemolymph volume. Cautery of the mNSC, provided it is performed within 3 h of emergence, results in a low protein concentration but has no effect on the haemolymph volume. The observations are discussed in terms of the corpora allata and mNSC control of haemolymph protein synthesis.

Total protein content and protein synthesis within pre-elongation stage bovine embryos

1998 ◽  
Vol 50 (2) ◽  
pp. 139-145 ◽  
Author(s):  
J.G. Thompson ◽  
A.N.M. Sherman ◽  
N.W. Allen ◽  
L.T. McGowan ◽  
H.R. Tervit
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Total Protein ◽  
Total Protein Content ◽  
Bovine Embryos

scholarly journals A Critical Appraisal of Current Practice in the Detection, Analysis, and Reporting of Cryoglobulins

2008 ◽  
Vol 54 (1) ◽  
pp. 39-43 ◽  
Author(s):  
Pieter Vermeersch ◽  
Koenraad Gijbels ◽  
Godelieve Mariën ◽  
Rod Lunn ◽  
William Egner ◽  
...  
Keyword(s):  
Reference Values ◽  
Total Protein ◽  
Protein Concentration ◽  
Current Practice ◽  
Total Protein Content ◽  
Specific Reference ◽  
Detection Analysis ◽  
Standard Procedures ◽  
Comparability Of Results ◽  
Missed Diagnoses

Abstract To assess current practice in the detection, analysis, and reporting of cryoglobulins, a questionnaire was sent to 140 laboratories. Only 36% of laboratories used standard procedures (tube preheating, transport in container, and sedimentation and/or centrifugation at 37 °C) to ensure that the temperature did not drop below 37 °C until after serum separation. Time periods allowed for cryoprecipitation at 4 °C varied from 12 h to 9 days, with 30% of laboratories allowing precipitation for <3 days. After cryoprecipitation, 81% of laboratories resolubilized the cryoprecipitate at 37 °C, and 77% further immunotyped the cryoprecipitate. After analysis, 5% referred the sample for confirmation, 58% provided a nonquantitative report, and 37% reported the cryoglobulin concentration in the cryoprecipitate as cryocrit, total protein concentration, and/or immunoglobulin concentration. Only 3 laboratories (2%) provided cryoprecipitate-specific reference values for total protein content, and none provided reference values for immunoglobulins. We believe standardization is needed for cryoglobulin detection to avoid missed diagnoses and improve the comparability of results. Laboratories should ensure that sample temperature does not drop below 37 °C until after serum separation. The serum should cryoprecipitate at 4 °C for at least 3 (preferably 7) days. The cryoprecipitate should be washed and resolubilized at 37 °C for further analysis.

In vitro Na+, K+-ATPase (EC 3.6.1.3)-dependent respiration and protein synthesis in skeletal muscle of pigs fed at three dietary protein levels

1989 ◽  
Vol 61 (3) ◽  
pp. 453-465 ◽  
Author(s):  
O. Adeola ◽  
L. G. Young ◽  
B. W. Mcbride ◽  
R. O. Ball
Keyword(s):  
Protein Synthesis ◽  
Dietary Protein ◽  
Protein Concentration ◽  
Live Weight ◽  
Synthesis Rate ◽  
Sartorius Muscle ◽  
Close Link ◽  
Protein Levels ◽  
Daily Gain

1. Eighteen pigs were offered diets containing 130, 170 or 210 g protein/kg with three barrows and three gilts per diet from 20 to 60 kg live weight. Oxygen consumption, Na1, K1-ATPase (EC 3·6·1· 3)-dependent and -independent respiration and protein synthesis were measured in vitro in intercostal and sartorius muscle preparations from these pigs.2. Increasing dietary protein concentration increased (P < 0·01) daily gain and dissectible muscle in carcass.3. O2 consumption and Na+, K+-ATPase-dependent respiration of the intercostal and sartorius muscles increased linearly (P < 0·01) with increase in dietary protein concentration. The requirement for the support of the transport of Na+ and K+ across the cell membrane in these muscles, on average, accounted for 22–25% of the O2 consumption.4. Synthesis rate (mg/g per d) of protein in the sartorius muscle increased (P < 0·05) from 3·05 to 5·07 and increased (P < 0·1) from 2·57 to 4.06 in the intercostal muscle as dietary protein increased from 130 to 210 g/kg diet.5. Regression of Na+, K+-ATPase-dependent respiration against protein synthesis in each of intercostal and sartorius muscles showed a linear relation, an attestation of a close link between productive processes and auxiliary energy expenditure.

scholarly journals Individual Acclimatization of Apis mellifera L. to the Thermal Homeostasis of the Colony

Sociobiology ◽  
2019 ◽  
Vol 66 (1) ◽  
pp. 81
Author(s):  
Marcos Venâncio Lima ◽  
Leonardo Augusto Fonseca Pascoal ◽  
Edilson Paes Saraiva ◽  
Kilmer Oliveira Soares ◽  
João Paulo Araújo Fernandes de Queiroz ◽  
...  
Keyword(s):  
Apis Mellifera ◽  
Surface Temperature ◽  
Total Protein ◽  
Protein Concentration ◽  
Climate Changes ◽  
Global Climate ◽  
Total Protein Content ◽  
Biological Processes ◽  
Total Protein Concentration ◽  
Global Climate Changes

Bees play an important role in maintaining biodiversity by promoting the pollination of numerous plant species. Recent global climate changes are affecting the average air temperature, thereby altering the biological processes of many species. The objective of this study was to evaluate the adaptation of Apis mellifera L. bees to temperature increases and their responses to thermal homeostasis in the colony. Research was performed at the Federal University of Paraíba Laboratory of Bees using three treatments: Control, 33 °C and 40 °C. For the latter two treatments, colonies were kept in a 24 m² climate chamber with an opening at the hive entrance, giving the bees access to the outside environment. The following parameters were evaluated: difference between internal and external hive temperature, thorax surface temperature and total protein concentration in the hemolymph. Internal colony temperature varied according to the external hive temperature. Nurse bees that care for larvae exhibited higher heat production, expressed as thorax surface temperature. Total protein content in the hemolymph was highest in the 40 °C treatment and decreased with ambient temperature. External hive temperature influences internal hive temperature, and nurse bees have higher capacities for thermogenesis.

Protein synthesis and degradation in flight muscles of adult crickets (Gryllus bimaculatus)

1995 ◽  
Vol 198 (5) ◽  
pp. 1071-1077 ◽  
Author(s):  
T Gomi ◽  
T Okuda ◽  
S Tanaka
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Total Protein ◽  
Muscle Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Adult Life ◽  
Total Protein Content ◽  
Gryllus Bimaculatus ◽  
Flight Muscles

The development and degeneration of the flight muscles in adult crickets, Gryllus bimaculatus, were studied (1) by determination of the total protein content, (2) by SDS one-dimensional polyacrylamide gel electrophoresis (SDS&shy;PAGE) of muscle protein and (3) by in vitro culturing of the muscle. The total protein content of the dorso-longitudinal muscle (DLM) and metathoracic dorso-ventral muscle (DVM) increased during the early days of adult life in both sexes. This high protein content was maintained for at least a further 10 days in some individuals, while in others it declined to a low level. Mesothoracic DVMs in males also showed an increase in protein content after adult emergence but did not undergo histolysis, whereas those in females showed no significant temporal change in protein content. Removal of hind wings or artificial de-alation was found to be useful in inducing degeneration of DLMs and metathoracic DVMs. This treatment also stimulated ovarian development in females. An analysis by SDS&shy;PAGE provided no evidence for new protein synthesis prior to or during flight muscle degeneration. A high rate of [3H]- or [35S]methionine incorporation was observed in DLMs taken from newly emerged adults, but, in intact crickets, the rate declined rapidly during the first 3 days of adult life, a pattern consistent with that obtained from the measurement of total protein content. Compared with DLMs removed from intact crickets, DLMs taken from de-alated crickets showed reduced rates of protein synthesis during in vitro culturing. This, together with the onset of protein degradation, appears to cause the rapid decrease in total protein content of the muscle in de-alated crickets.

The Relationships Between Nutrition, Hormones and Reproduction in the Blowfly Calliphora Erythrocephala (Meig.)

1961 ◽  
Vol 38 (3) ◽  
pp. 637-646
Author(s):  
J. STRANGWAYS-DIXON
Keyword(s):  
Gravid Female ◽  
Neurosecretory Cells ◽  
Volume Activity ◽  
Calliphora Erythrocephala ◽  
Carbohydrate Consumption ◽  
Low Protein ◽  
Low Carbohydrate ◽  
Protein Selection ◽  
Median Neurosecretory Cells ◽  
Reproductive Cycles

1. A study has been made of the effects of removal of ovaries, copora allata (c.a.) and median neurosecretory cells (m.n.c.) upon the selection by female blowflies of carbohydrate (sugar in water) or ‘protein’ (Marmite in milk). 2. Extirpation of the ovaries resulted in high carbohydrate-low protein selection and in hypertrophy of the c.a. 3. Extirpation of the c.a. resulted in low carbohydrate selection. 4. Extirpation of both ovaries and c.a. resulted in low carbohydrate selection. 5. These and other results suggest that selection is independent of direct ovarian control, but that the ovaries influence selection in that they utilize the ingested foods and thus bring about the succession of feeding cycles. 6. The c.a., whose volume (activity?) changes cyclically during each cycle of reproduction, appears to control the fluctuations in carbohydrate consumption. 7. The m.n.c. seem to be necessary for the ingestion of ‘protein’ and for the activity of the c.a. 8. Reproductive cycles tend to overlap. The succeeding cycle in a gravid female must be taken into consideration when events are being related to reproduction.

scholarly journals Chemical characterization of Brazilian hulless barley varieties, flour fractionation, and protein concentration

2004 ◽  
Vol 61 (6) ◽  
pp. 593-597 ◽  
Author(s):  
Cristiane Vieira Helm ◽  
Alicia de Francisco
Keyword(s):  
Chemical Composition ◽  
Protein Content ◽  
Total Protein ◽  
Protein Concentration ◽  
Chemical Characterization ◽  
Total Protein Content ◽  
Human Consumption ◽  
Published Data ◽  
Protein Nitrogen ◽  
Hulless Barley

Even though hulless barley is widely known due to its nutritional potential, in Brazil it is only grown at a few agricultural experimental stations. There is no published data about the chemical composition of Brazilian hulless barley varieties; however, research laboratories have studied their agronomical characteristics. The objectives of this study were to present the chemical characterization and effect of flour fractionation on protein concentration of six Brazilian hulless barley varieties, namely IAC IBON 214/82, IAC 8612/421, IAC 8501/31, IAC 8501/12, IAPAR 39-Acumaí, and IAC 8501/22. The analyses included: ash, ether extract, total protein, starch, total insoluble and soluble dietary fiber, and beta-glucans. Flour fractionation was carried out by sieving. The flour fractions were evaluated for crude protein, protein, and protein and non-protein nitrogen. Chemical composition varied (P < 0.05) among all the varieties. IAC 8501/22, IAC 8501/31, and IAC 8501/12 showed the highest protein content (15.69, 15.25, and 14.94% respectively). Differences (P < 0.05) among the protein of the fractionated flours were detected, and might be attributed primarily to genetic background since all varieties were grown under the same environmental conditions. Fractionating the flour increased the total protein content, in some fractions, by up to 2%. These results may be useful in the food industry for the selection of hulless barley varieties for human consumption and to produce substantially protein-enriched flour fractions.

Morphology and histology of the endocrine glands of Zootermopsis angusticollis Hagen (Isoptera)

1972 ◽  
Vol 50 (12) ◽  
pp. 1537-1547 ◽  
Author(s):  
Cedric Gillott ◽  
Chih-Ming Yin
Keyword(s):  
Cell Types ◽  
Cell Number ◽  
Neurosecretory Cells ◽  
Corpora Allata ◽  
Endocrine Glands ◽  
Histological Changes ◽  
Secretory Cycle ◽  
Zootermopsis Angusticollis ◽  
Primary Reproductives ◽  
Median Neurosecretory Cells

The morphology and histology of the endocrine glands of the various castes of Zootermopsis angmticollis were examined. Six types of median neurosecretory cells are distinguishable by size and stain affinity. No differences in the relative numbers of these cell types among castes can be seen. It is postulated that they may be different forms of the same cell during its synthetic and secretory cycle. Lateral neurosecretory cells can be identified consistently only in mature primary reproductives of both sexes. In the corpora cardiaca two types of cells occur; the fuchsinophilic cells are distributed generally whereas the cells that take up counterstain are restricted to the center of the gland. Intercellular neurosecretory cell product is found throughout the gland. No histological changes associated with the formation of particular castes were observed. The corpora allata (CA) vary in size and histological appearance according to caste but not sex. The CA of reproductives (primary and supplementary) and presoldiers are larger than those of juveniles of the same instar; those of soldiers are about the same size as those of the corresponding juvenile stage. These size increases are due mainly to changes in the ratio cytoplasmic diameter: nuclear diameter of the constituent cells and not to an increase in cell number. The H-shaped molt glands, which, as in other pterygote insects, disappear within a few days of the imaginal molt, are composed of a large prothoracic portion and a smaller cephalic ('ventral gland') portion extending anteriorly and dorsally. Histologically the two components are indistinguishable. Running through the glands are thin strands of muscle.

Decrease of VEGF within malignant ascites during catumaxomab treatment: Results from a pivotal phase II/III study

2009 ◽  
Vol 27 (15_suppl) ◽  
pp. 3029-3029
Author(s):  
M. Jäger ◽  
A. Schoberth ◽  
B. Theissen ◽  
J. Hess ◽  
H. Friccius-Quecke ◽  
...  
Keyword(s):  
Tumor Cell ◽  
Phase Ii ◽  
Total Protein ◽  
Protein Concentration ◽  
Malignant Ascites ◽  
Control Group ◽  
Pivotal Phase ◽  
Protein Ratio ◽  
Protein Levels ◽  
Vegf Protein

3029 Background: Treatment with the trifunctional anti-EpCAM x anti-CD3 antibody catumaxomab efficiently eliminates tumor cells from the peritoneal cavity (Jäger et al., ASCO 2007) and led to clinically relevant prolongation of puncture-free survival (PuFS) in patients with malignant ascites (MA) in a pivotal phase II/III trial (Parsons et al., ASCO 2008). As vascular endothelial growth factor (VEGF) levels are markedly elevated in MA in comparison to cirrhotic ascites the question was addressed whether catumaxomab treatment impacts the expression or accumulation of VEGF within MA. Here we report that in addition to tumor cell depletion, VEGF protein levels in MA significantly decreased upon catumaxomab therapy. We propose that the strongly correlated tumor cell elimination and reduced VEGF protein levels are causative for the prolonged PuFS of patients suffering from MA. Methods: VEGF and total protein levels were measured by ELISA and BCA from MA supernatants before catumaxomab therapy, after the 1st infusion (10μg; day 3) and after the 4th infusion (150μg; day 11). Data were statistically analysed for the ratio of the VEGF protein concentration versus the total protein concentration for the MA treatment groups with ovarian (OC) or nonovarian cancer (NC) as underlying disease and the corresponding control groups that received paracentesis only. Results: One day after the last catumaxomab infusion 46 or 47 patients analysed in the OC or NC treatment group showed a statistically significant decrease in VEGF to total protein ratio when compared to the measurement before catumaxomab therapy (ANOVA p=0.034 for OC and p<0.001 for NC). These results are consistent with the tumor cell elimination previously assessed in these patients. In contrast, the OC control group showed a statistically significant increase of VEGF to total protein ratio (p=0.009), which is accompanied by an increase in tumor cell numbers. In the NC control group VEGF to total protein ratio remained unaffected (p=0.096). Conclusions: Catumaxomab therapy significantly reduced VEGF protein levels correlating with tumor cell elimination in MA, which in turn led to the prevention of fluid accumulation in the peritoneal cavity and finally to prolonged PuFS of patients suffering from MA. [Table: see text]

Protein Levels Affect the Cure Efficiency and Allergenic Potential of Polyisoprene Latices

2006 ◽  
Vol 79 (4) ◽  
pp. 631-640 ◽  
Author(s):  
W. W. Schloman ◽  
V. H. Teetor ◽  
D. T. Ray
Keyword(s):  
Total Protein ◽  
Crosslink Density ◽  
Rubber Particle ◽  
Particle Surface ◽  
Total Protein Content ◽  
Ionic Surfactant ◽  
Protein Levels ◽  
Allergenic Potential ◽  
Extractable Protein ◽  
The Cost

Abstract Commercial NR latex has a higher total protein content than guayule (GR) latex. Some NR proteins are allergens bound to the rubber particle surface. Washing NR latex with a non-ionic surfactant displaced these particle-bound proteins and reduced allergens by more than 95%. The cost of such deproteination was reduced vulcanization efficiency, as determined by crosslink density. The extent of vulcanization correlated well with both total protein and allergen levels. Compared with films prepared from untreated NR latex, films from both surfactant-treated NR latex and GR latex had lower states of cure. Where particle-bound proteins were still present, as they are in GR latex, crosslink development could be completed by heat aging. In contrast, crosslink development in the film from surfactant-treated NR was complete after dipping and drying. The resulting films yielded high levels of extractable protein allergens.

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