Supplemental Feed Protein Concentration and Weaning Age Affects Replacement Beef Heifer Performance

Abstract Development of resistance during multiple foulings and three-step Cleaning-In-Place (CIP) operations, simulating an industrial cleaning regime of polysulfone ultrafiltration membranes, was investigated. The study explored how trans-membrane pressure (150 and 300 kPa) and feed protein concentration (0.9 and 10%) influenced resistance reduction during filtration and flux recovery by the cleaning procedures. New membranes, pre-cleaned with a full CIP cycle, were used for each experiment. Subsequent fouling (simulating production) and CIP were done three times in a row and the development of fouling layer resistance was monitored and evaluated. Results show that filtration performance decreased during the first days of usage, possibly related to build-up of internal fouling. Cleaning success based on flux recovery was negatively influenced by a high protein concentration in the feed, but independent of the trans-membrane pressure during filtration.

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Albumin-Induced Endocytic Vacuoles in Tetrahymena Pyrijormis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100117091 ◽

1975 ◽

Vol 33 ◽

pp. 694-695

Author(s):

L. J. Brenner ◽

D. G. Osborne ◽

B. L. Schumaker

Keyword(s):

Electron Microscopy ◽

Bovine Serum Albumin ◽

Bovine Serum ◽

Protein Concentration ◽

Tetrahymena Pyriformis ◽

Sequence Of Events ◽

Cytoplasmic Bodies ◽

Food Vacuoles ◽

Mouse Ascites ◽

Normal Human

Exposure of the ciliate, Tetrahymena pyriformis, strain WH6, to normal human or rabbit sera or mouse ascites fluids induces the formation of large cytoplasmic bodies. By electron microscopy these (LB) are observed to be membrane-bounded structures, generally spherical and varying in size (Fig. 1), which do not resemble the food vacuoles of cells grown in proteinaceous broth. The possibility exists that the large bodies represent endocytic vacuoles containing material concentrated from the highly nutritive proteins and lipoproteins of the sera or ascites fluids. Tetrahymena mixed with bovine serum albumin or ovalbumin solutions having about the same protein concentration (7g/100 ml) as serum form endocytic vacuoles which bear little resemblance to the serum-induced LB. The albumin-induced structures (Fig. 2) are irregular in shape, rarely spherical, and have contents which vary in density and consistency. In this paper an attempt is made to formulate the sequence of events which might occur in the formation of the albumin-induced vacuoles.

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Monoamine Oxidase and Other Mitochondrial Enzymes in Density Subpopulations of Human Platelets

Thrombosis and Haemostasis ◽

10.1055/s-0038-1642560 ◽

1988 ◽

Vol 59 (01) ◽

pp. 029-033 ◽

Cited By ~ 10

Author(s):

K G Chamberlain ◽

D G Penington

Keyword(s):

Monoamine Oxidase ◽

Protein Concentration ◽

Close Correlation ◽

Human Platelets ◽

Mitochondrial Enzymes ◽

Density Fractions ◽

Percoll Gradients ◽

Normal Human ◽

The Mean ◽

Very High

SummaryNormal human platelets have been separated according to density on continuous Percoll gradients and the platelet distribution divided into five fractions containing approximately equal numbers of platelets. The mean volumes and protein contents of the platelets in each fraction were found to correlate positively with density while the protein concentration did not differ significantly between the fractions. Four mitochondrial enzymes (monoamine oxidase, glutamate dehydrogenase, cytochrome oxidase and NADP-dependent isocitrate dehydrogenase) were assayed and their activities per unit volume were found to increase in a very similar monotonie fashion with platelet density. When MAO and GDH were assayed on the same set of density fractions the correlation between the two activities was very high (r = 0.94–1.00, p <0.001) and a similar close correlation was found between MAO and ICDH. The results support the hypothesis that high density platelets either have a higher concentration of mitochondria or have larger mitochondria than low density platelets.

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Does Low Protein Concentration of Tissue-type Plasminogen Activator Predict a Low Risk of Spontaneous Deep Vein Thrombosis?

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649803 ◽

1995 ◽

Vol 74 (02) ◽

pp. 718-721 ◽

Cited By ~ 8

Author(s):

Jørgen Gram ◽

Johannes Sidelmann ◽

Jørgen Jespersen

Keyword(s):

Deep Vein Thrombosis ◽

Confidence Interval ◽

Plasminogen Activator ◽

Fibrinolytic Activity ◽

Protein Concentration ◽

Tissue Type ◽

Vein Thrombosis ◽

Low Protein ◽

Deep Vein ◽

Pai 1

SummaryMany reports have demonstrated an abnormal fibrinolysis in a subset of patients with deep vein thrombosis. We have studied systemic global fibrinolytic activity and protein concentrations of tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor type 1 (PAI-1) in plasma of 25 young patients with a previous instance of spontaneous deep vein thrombosis documented by phlebography and in 50 healthy controls. The two populations were comparable with respect to a number of base-line variables (age, height, weight, etc.), while the patients had significantly lower fibrinolytic activity (p <0.02), and significantly higher protein concentrations of t-PA (p <0.0001) and PAI-1 (p <0.0006).We used probit scale plots to identify the consequence of different cut-off points to separate patients from controls. Reasonable separation could be obtained for t-PA with a cut-off point of 5.2 ng/ml and for PAI-1 18 ng/ml. The sensitivity and specificity for these cut-off points were for t-PA 73% (95% confidence interval 63%-84%) and for PAI-1 67% (confidence interval 55%-77%). The negative predictive value with a cut-off point t-PA concentration of 5.2 ng/ml was 85% (95% confidence interval 70%-94%). We observed a significantly negative association between concentration of t-PA and fibrinolytic activity (rs = -0.47; p <0.005) and also between PAI-1 and fibrinolytic activity (rs = -0.78; p <0.005).We conclude that a young healthy population is characterized by low protein concentration of t-PA (and PAI-1) compared with young patients with a previous instance of spontaneous vein thrombosis, and we tentatively state that a low protein concentration of t-PA predicts a low risk of spontaneous deep vein thrombosis.

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Additional nutritional considerations for preconditioning beef calves.

EDIS ◽

10.32473/edis-an334-2017 ◽

2017 ◽

Vol 2017 (4) ◽

Author(s):

Philipe Moriel

Keyword(s):

Average Daily Gain ◽

Beef Steers ◽

Labor Costs ◽

Vaccine Response ◽

Negative Effects ◽

Beef Calves ◽

Supplemental Feed ◽

Concentrate Supplementation ◽

Protein Supply ◽

Daily Gain

Calves can be preconditioned using a wide variety of supplemental feed ingredients. However, feed ingredient selection is not the only factor to consider during a preconditioning process. Increasing the protein supply to stressed, preconditioning beef steers led to greater growth performance, and increased immune response to vaccination during a 42-day preconditioning period. Producers should not reduce the frequency of concentrate supplementation during the entire preconditioning period as it might lead to poorer vaccine response and average daily gain (consequently, less calf value at sale). However, a gradual reduction of frequency of supplementation is a supplementation strategy that can overcome these negative effects on growth and immunity, and allows producers to save on feeding and labor costs without producing lighter calves that have weaker immune responses.

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Extraction and Partial Purification of Protease from Bilimbi (Averrhoa bilimbi L.)

Scientific Research Journal ◽

10.24191/srj.v10i2.9403 ◽

2013 ◽

Vol 10 (2) ◽

pp. 29

Author(s):

Normah Ismail ◽

Nur' Ain Mohamad Kharoe

Keyword(s):

Molecular Weight ◽

Protein Content ◽

Ammonium Sulfate ◽

Molecular Weight Distribution ◽

Weight Distribution ◽

Protease Activity ◽

Protein Concentration ◽

Temperature Stability ◽

Partial Purification ◽

Ammonium Sulfate Precipitation

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage.

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