Reversible heat coagulation of some water-soluble amino acid copolymers

1957 ◽  
Vol 23 (104) ◽  
pp. 843-849 ◽  
Author(s):  
Junzo Noguchi ◽  
Tadao Hayakawa ◽  
Mituo Ebata
Keyword(s):  
2019 ◽  
Vol 97 (Supplement_2) ◽  
pp. 82-83
Author(s):  
Pornpim Aparachita ◽  
Scott Carter ◽  
Afton Sawyer ◽  
Jared Harshman ◽  
Zach Rambo ◽  
...  

Abstract Previously, we reported that supplementing a water soluble zinc via drinking water (0 to 80 mg/L) to nursery pigs improved ADG and G:F. To evaluate the efficacy of higher titrated levels of this water soluble zinc amino acid complex (ProPath®Zn LQ, Zinpro Corporation, Eden Prairie, MN) on growth performance, 280 crossbred pigs (5.5 kg BW; 19 d of age) were randomly allotted to four water treatments (7 pens/treatment; 10 pigs/pen). The water treatments were 0, 40, 80 and 160 mg Zn/L of water. Pigs were fed in 4 dietary phases with complex, nutrient-dense, corn-soybean meal-based diets: Phase 1 and 2 (2,500 and 1,750 mg Zn as ZnO/kg; d 1–7 and 7–14, respectively) and Phase 3 and 4 (200 mg Cu as CuSO4/kg; d 14–23 and 23–42, respectively). Pigs and feeders were weighed weekly to determine ADG, ADFI, and G:F. Water meters were used to record and calculate water disappearance and zinc intake. Data were analyzed as a randomized complete block design. Orthogonal polynomial contrasts were used to determine linear and curvilinear effects. Water and total zinc intake increased linearly (P < 0.001) with increasing water zinc concentration. From d 0–14 when high dietary zinc was fed, there were no differences (P > 0.10) in ADG, ADFI, or G:F. However, from d 14–42 when basal levels of zinc were fed, quadratic improvements in ADG (0.545, 0.561, 0.578, 0.546 kg; P < 0.05) and G:F (0.686, 0.706, 0.723, 0.702; P < 0.01) were observed with increasing zinc via water. Similarly for d 0–42, ADG (0.435, 0.440, 0.454; 0.434 kg; P = 0.07), G:F (0.726, 0.740, 0.763, 0.749; P = 0.05) and average ending wt (23.73, 23.97, 24.55, 23.70 kg; P = 0.07) improved quadratically with increasing zinc. In conclusion, supplementing ProPath®Zn LQ via water resulted in improvements in ADG and G:F for nursery pigs.


1996 ◽  
Vol 61 (22) ◽  
pp. 7650-7651 ◽  
Author(s):  
Christopher L. Wysong ◽  
T. Scott Yokum ◽  
Guillermo A. Morales ◽  
Rebekah L. Gundry ◽  
Mark L. McLaughlin ◽  
...  

1993 ◽  
Vol 115 (9) ◽  
pp. 3790-3791 ◽  
Author(s):  
Humberto Diaz ◽  
Kwok Yin Tsang ◽  
Danny Choo ◽  
Jose R. Espina ◽  
Jeffery W. Kelly

2019 ◽  
Vol 30 (1) ◽  
pp. 247-249 ◽  
Author(s):  
Xingjie Zhang ◽  
Zhi Meng ◽  
Zhiqiang Ma ◽  
Junhong Liu ◽  
Guiyan Han ◽  
...  

Pharmaceutics ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 941
Author(s):  
Melvin Wostry ◽  
Hanna Plappert ◽  
Holger Grohganz

Freeze-drying was evaluated as a production technique for co-amorphous systems of a poorly water-soluble drug. Naproxen was freeze-dried together with arginine and lysine as co-former. To increase the solubility of naproxen in the starting solution, the applicability of five surfactants was investigated, namely sodium dodecyl sulfate, pluronic F-127, polyoxyethylene (40) stearate, tween 20 and TPGS 1000. The influence of the surfactant type, surfactant concentration and total solid content to be freeze-dried on the solid state of the sample was investigated. X-ray powder diffraction and differential scanning calorimetry showed that the majority of systems formed co-amorphous one-phase systems. However, at higher surfactant concentrations, and depending on the surfactant type, surfactant reflections were observed in the XRPD analysis upon production. Crystallization of both naproxen and amino acid occurred from some combinations under storage. In conclusion, freeze-drying was shown to be a feasible technique for the production of a selection of co-amorphous drug–amino acid formulations.


1962 ◽  
Vol 40 (1) ◽  
pp. 459-469 ◽  
Author(s):  
P. H. Jellinck ◽  
Louise Irwin

Aerobic incubation of estrone-16-C14with peroxidase in the presence of serum albumin and other proteins resulted in the formation of water-soluble, ether-insoluble metabolites in high percentage yields. Similar products were formed when protein was replaced by cysteine or tryptophan but none of the other amino acids tested had any effect. The evidence points to an initial generation of hydrogen peroxide from these nitrogenous compounds by the enzyme acting as an aerobic oxidase, and the subsequent peroxidation of estrone to highly reactive products. These then combine with the protein or amino acid or else undergo alternative reactions. A strong chemical bond is formed with albumin and attempts to release the estrone metabolites from it were unsuccessful. Uterine homogenates from estrogen-treated rats showing high DPNH oxidase activity contained no "peroxidase" as measured by the formation of water-soluble products from estrone in the presence of protein.


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