scholarly journals Differences in Nutritional Value of Various Fish Products Expressed by the Amino Acid Profiles of their Water-soluble Fractions

2019 ◽  
Vol 4 (4) ◽  
pp. 1-5
Keyword(s):  
Amino Acid ◽  
Fish Species ◽  
Soluble Fraction ◽  
Amino Acid Content ◽  
Water Soluble ◽  
Fish Products ◽  
Water Soluble Fraction ◽  
Edible Tissues ◽  
Amino Acid Profiles ◽  
Branched Chain

The amino acid profiles of the whole water-soluble fraction of some popular fish products (muscle and caviar) have been studied. The pike (Esox lucius) muscle and caviar contain more branched-chain amino acids than all the products being studied including some valuable sturgeon and salmon fish species, and pike muscle also contains the highest amount of phenylalanine and lysine. Pike caviar is also a leader in threonine content. The pike may be considered as one of the most nutritionally valuable fish species, especially if the full amino acid content from the water-soluble fraction of its edible tissues is compared.

Metabolism of EPTC in Corn (Zea mays)

Weed Science ◽  
1978 ◽  
Vol 26 (2) ◽  
pp. 157-160 ◽  
Author(s):  
R. D. Carringer ◽  
C. E. Rieck ◽  
L. P. Bush
Keyword(s):  
Zea Mays ◽  
Enzyme Activity ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Soluble Fraction ◽  
Degradation Products ◽  
Reduced Glutathione ◽  
Water Soluble ◽  
Glutathione Conjugate ◽  
Water Soluble Fraction

EPTC (S-ethyl dipropylthiocarbamate) metabolism in corn (Zea mays L. ‘inbred B37’) was studied utilizing carbonyl-14C-EPTC and propyl-1-14C-EPTC. Two radioactive compounds were found in the organic-soluble fraction, namely, EPTC and EPTC-sulfoxide. Five metabolites were found in the water-soluble fraction. Amino acid analysis indicated that one water-soluble metabolite was a glutathione conjugate [S-(N,N-dipropylcarbamyl)glutathione] and that three other metabolites were probably degradation products of the glutathione conjugate. It was determined that EPTC-sulfoxide reacts chemically with reduced glutathione, yielding the conjugate. There was no detectable glutathione S-transferase enzyme activity associated with the sulfoxide cleavage.

scholarly journals Alteration of serum amino acid profiles by dietary adenine supplementation inhibits fatty liver development in rats

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hiroki Nishi ◽  
Daisuke Yamanaka ◽  
Masato Masuda ◽  
Yuki Goda ◽  
Koichi Ito ◽  
...  
Keyword(s):  
Amino Acid ◽  
Fatty Liver ◽  
Causative Factor ◽  
Amino Acid Profile ◽  
Liver Development ◽  
Concentration Data ◽  
Amino Acid Profiles ◽  
Arginine Deficiency ◽  
Branched Chain ◽  
Tag Accumulation

AbstractStudies on animal models have demonstrated that feeding a low-arginine diet inhibits triacylglycerol (TAG) secretion from the liver, resulting in marked fatty liver development in rats. Here, we first showed that culturing hepatocytes in the medium mimicking the serum amino acid profile of low-arginine diet-fed rats induced TAG accumulation in the cells, indicating that the specific amino acid profile caused TAG accumulation in hepatocytes. Dietary adenine supplementation completely recovered hepatic TAG secretion and abolished hepatic TAG accumulation in rats. A comprehensive non-linear analysis revealed that inhibition of hepatic TAG accumulation by dietary adenine supplementation could be predicted using only serum amino acid concentration data. Comparison of serum amino acid concentrations indicated that histidine, methionine, and branched-chain amino acid (BCAA) concentrations were altered by adenine supplementation. Furthermore, when the serum amino acid profiles of low-arginine diet-fed rats were altered by modifying methionine or BCAA concentrations in their diets, their hepatic TAG accumulation was abolished. Altogether, these results suggest that an increase in methionine and BCAA levels in the serum in response to dietary arginine deficiency is a key causative factor for hepatic TAG accumulation, and dietary adenine supplementation could disrupt this phenomenon by altering serum amino acid profiles.

Impact of Rice Flour Cold-Water-Soluble Fraction Removal on Gelatinization and Pasting Properties

2014 ◽  
Vol 91 (5) ◽  
pp. 473-481 ◽  
Author(s):  
Guiai Jiao ◽  
Xiangjin Wei ◽  
Gaoneng Shao ◽  
Lihong Xie ◽  
Zhonghua Sheng ◽  
...  
Keyword(s):  
Cold Water ◽  
Soluble Fraction ◽  
Rice Flour ◽  
Pasting Properties ◽  
Water Soluble ◽  
Water Soluble Fraction

FRACTIONATION OF LIVETIN AND THE MOLECULAR WEIGHTS OF THE α- AND β-COMPONENTS

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook
Keyword(s):  
Light Scattering ◽  
Soluble Protein ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Water Soluble ◽  
Water Soluble Fraction ◽  
Molecular Weights ◽  
Water Soluble Protein ◽  
Hen Egg Yolk ◽  
Hen Egg

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.

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