scholarly journals Availability to pigs of amino acids in cereal grains

1981 ◽  
Vol 46 (1) ◽  
pp. 173-180 ◽  
Author(s):  
M. R. Taverner ◽  
D. J. Farrell

1. Availability values for amino acids in nine cereal grains determined by faecal analyses with pigs and by the Silcock available lysine test (Roach et al. 1967) and an in vitro digestibility assay were compared with ileal availability values for the same grains determined with pigs by Taverner et al. (1981b).2. There was a significant canonical correlation of ileal and faecal availability values. On average, apparent faecal availability of the indispensable amino acids was 4·2% greater than apparent ileal availability, but the difference was up to 12·6% for threonine. Furthermore, the difference appeared to increase as the digestibility of the grain decreased.3. Silcock available-lysine values for the cereal grains were unrelated to the lysine truly absorbed by the pig.4. There were close relationships of ileal protein and lysine availability values on nitrogen digestibility determined by an in vitro assay using pronase enzyme.

1981 ◽  
Vol 46 (1) ◽  
pp. 181-192 ◽  
Author(s):  
M. R. Taverner ◽  
D. J. Farrell

1. Protein digestibility and lysine availability were determined in a range of grain samples using an in vitro digestibility assay calibrated with ileal digestibility values.2. Mean(± SE) values predicted for nitrogen digestibility were 0·92±0·011 in wheat and 0·88±0·021 in barley, and the predicted lysine availability in wheat was 0·86±0·021.3. Chemical and physical characteristics of the grains were determined and those most closely associated with protein digestibility for wheat were the contents of hemicellulose, neutral-detergent fibre, the bulk density, and to a lesser extent, N and acid-detergent fibre contents. These relationships were used to determine prediction equations for the available lysine content of wheat.


1968 ◽  
Vol 20 (03/04) ◽  
pp. 384-396 ◽  
Author(s):  
G Zbinden ◽  
S Tomlin

SummaryAn in vitro system is described in which adhesion of blood platelets to washed and tannic acid-treated red cells was assayed quantitatively by microscopic observation. ADP, epinephrine and TAME produced a reversible increase in platelet adhesiveness which was antagonized by AMP. With Evans blue, polyanetholsulfonate, phthalanilide NSC 38280, thrombin and heparin at concentrations above 1-4 u/ml the increase was irreversible. The ADP-induced increase in adhesiveness was inhibited by sodium citrate, EDTA, AMP, ATP and N-ethylmaleimide. EDTA, AMP and the SH-blocker N-ethylmaleimide also reduced spontaneous platelet adhesion to red cells. No significant effects were observed with adenosine, phenprocoumon, 5-HT, phthalanilide NSC 57155, various estrogens, progestogens and fatty acids, acetylsalicylic acid and similarly acting agents, hydroxylamine, glucose and KCN. The method may be useful for the screening of thrombogenic and antithrombotic properties of drugs.


2021 ◽  
pp. 1-9
Author(s):  
Anita Virtanen ◽  
Outi Huttala ◽  
Kati Tihtonen ◽  
Tarja Toimela ◽  
Tuula Heinonen ◽  
...  

<b><i>Objective:</i></b> To determine the direct effect of pravastatin on angiogenesis and to study the interaction between pravastatin and maternal sera from women with early- or late-onset pre-eclampsia (PE), intrauterine growth restriction, or healthy pregnancy. <b><i>Methods:</i></b> We collected 5 maternal serum samples from each group. The effect of pravastatin on angiogenesis was assessed with and without maternal sera by quantifying tubule formation in a human-based in vitro assay. Pravastatin was added at 20, 1,000, and 8,000 ng/mL concentrations. Concentrations of angiogenic and inflammatory biomarkers in serum and in test medium after supplementation of serum alone and with pravastatin (1,000 ng/mL) were measured. <b><i>Results:</i></b> Therapeutic concentration of pravastatin (20 ng/mL) did not have significant direct effect on angiogenesis, but the highest concentrations inhibited angiogenesis. Pravastatin did not change the levels of biomarkers in the test media. There were no changes in angiogenesis when therapeutic dose of pravastatin was added with maternal sera, but there was a trend to wide individual variation towards enhanced angiogenesis, particularly in the early-onset PE group. <b><i>Conclusions:</i></b> At therapeutic concentration, pravastatin alone or with maternal sera has no significant effect on angiogenesis, but at high concentrations the effect seems to be anti-angiogenic estimated by in vitro assay.


Lab on a Chip ◽  
2021 ◽  
Author(s):  
YUHAO QIANG ◽  
Jia Liu ◽  
Ming Dao ◽  
E Du

Red blood cells (RBCs) are subjected to recurrent changes in shear stress and oxygen tension during blood circulation. The cyclic shear stress has been identified as an important factor that...


1981 ◽  
Vol 36 (1-2) ◽  
pp. 30-34 ◽  
Author(s):  
Rainer Sütfeld ◽  
Rolf Wiermann

Abstract Chalcone synthase was isolated from both anthers of Tulipa cv. “Apeldoorn” and petals of Cosmos sulphureus Cav. After certain prepurification steps, the enzymes were further purified using gel chromatography on Sephadex G-200 followed by repeated hydroxylapatite absorption chromatography. Both the enzymes showed the same chromatographic properties. After gel chromatography as well as after the first hydroxylapatite fractionation, the reaction products appeared as flavanones. However, after the second hydroxylapatite step, production of chalcones was observed. Like the enzyme from tulip anthers, the synthase from Cosmos petals produced the correspondingly substituted chalcones when p-coumaroyl-CoA, caffeoyl-CoA and feruloyl-CoA, respectively, were used as substractes. In both the cases, the ratios of the different chalcones produced were found to be about the same. The appearance of chalcone synthesis in this in vitro assay is caused by the complete elimination of chalcone isomerase in the purification procedure. The importance of the isomerase for flavonoid biosynthesis, particularly in plant systems which are accumulating chalcones, is discussed.


2009 ◽  
Vol 191 (7) ◽  
pp. 2033-2041 ◽  
Author(s):  
Meriyem Aktas ◽  
Franz Narberhaus

ABSTRACT Agrobacterium tumefaciens requires phosphatidylcholine (PC) in its membranes for plant infection. The phospholipid N-methyltransferase PmtA catalyzes all three transmethylation reactions of phosphatidylethanolamine (PE) to PC via the intermediates monomethylphosphatidylethanolamine (MMPE) and dimethylphosphatidylethanolamine (DMPE). The enzyme uses S-adenosylmethionine (SAM) as the methyl donor, converting it to S-adenosylhomocysteine (SAH). Little is known about the activity of bacterial Pmt enzymes, since PC biosynthesis in prokaryotes is rare. In this article, we present the purification and in vitro characterization of A. tumefaciens PmtA, which is a monomeric protein. It binds to PE, the intermediates MMPE and DMPE, the end product PC, and phosphatidylglycerol (PG) and phosphatidylinositol. Binding of the phospholipid substrates precedes binding of SAM. We used a coupled in vitro assay system to demonstrate the enzymatic activity of PmtA and to show that PmtA is inhibited by the end products PC and SAH and the antibiotic sinefungin. The presence of PG stimulates PmtA activity. Our study provides insights into the catalysis and control of a bacterial phospholipid N-methyltransferase.


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