scholarly journals Species differences in the occurrence of copper-metallothionein in the particulate fractions of the liver of copper-loaded animals

1984 ◽  
Vol 219 (2) ◽  
pp. 539-546 ◽  
Author(s):  
R K Mehra ◽  
I Bremner
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sodium Dodecyl Sulphate ◽  
Metal Content ◽  
Species Differences ◽  
Sodium Dodecyl ◽  
Pig Liver

Large amounts of Cu-metallothionein were obtained by 2-mercaptoethanol and sodium dodecyl sulphate extractions of the particulate fractions of the liver of pigs given high-Cu2+ diets or rats injected with Cu2+. Three isoproteins were purified from pig liver and characterized on the basis of their physicochemical properties, metal content and amino acid composition. No such pool of Cu-metallothionein was present in the liver of Cu2+-loaded sheep or of rats given Cu2+-supplemented diets.

scholarly journals  Quality of rabbit meat and phyto-additives

2010 ◽  
Vol 28 (No. 3) ◽  
pp. 161-167 ◽  
Author(s):  
M.P. Simonová ◽  
Ľ. Chrastinová ◽  
J. Mojto ◽  
A. Lauková ◽  
R. Szábová ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Plant Extracts ◽  
Good Health ◽  
Good Alternative ◽  
Health State ◽  
Rabbit Meat

The consumption of healthy and nutritive food (rich in proteins and low in cholesterol and lipid contents) is a preferred factor with the contemporary consumers. In addition, natural alternatives are requested to replace the additives used up to now but recently banned. To reach the above given condition, phyto-additives represent a good alternative. The aim of this study was to examine the physicochemical properties and amino acid composition of rabbit meat after the enrichment of rabbit diet with oregano, sage, and Eleutherococcus senticosus extracts, and to make a comparison with the commercial product XTRACT and control samples (without plant extracts). The addition of oregano and sage extracts as well as El. senticosus in the rabbit diet positively influenced the physicochemical properties of rabbit meat by increasing its energy value (P < 0.05 – sage). Supplementing rabbits feed with oregano and sage extracts led to an improvement on the amino acid composition (P < 0.01; P < 0.001 – serine). These findings are also supported by the good health state of rabbits. Outgoing from these results, the diet enriched with the plant extracts is beneficial for the health state of rabbits involving the nutritional quality of rabbit meat in connection with consumers.

scholarly journals Separation and partial characterization of guinea-pig caseins

1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Exchange Chromatography

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.

SOME PROPERTIES OF APOFERRITIN ISOLATED FROM GUINEA PIG LIVER

1962 ◽  
Vol 40 (1) ◽  
pp. 983-987 ◽  
Author(s):  
Felix Friedberg
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Guinea Pigs ◽  
Dicarboxylic Acids ◽  
Acetate Buffer ◽  
Pig Liver ◽  
Guinea Pig Liver

Apoferritin isolated from livers of guinea pigs and characterized by a s°w,20 of 17.7 and a pI of 4.8 (in acetate buffer Γ/2 0.1) was hydrolyzed with 5.7 N HCl for 22 and 44 hours and its amino acid composition determined. The protein appears rich in dicarboxylic acids and in leucine. The content of sulphur-containing amino acids is fairly small.

scholarly journals Studies on the subunits of human myeloperoxidase

1984 ◽  
Vol 222 (3) ◽  
pp. 701-709 ◽  
Author(s):  
R L Olsen ◽  
C Little
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Molecular Mass ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Additional Species ◽  
Main Protein

The subunit composition of human myeloperoxidase was studied with the use of sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and gel filtration. The subunit pattern observed depended on the manner in which the enzyme was treated before analysis. Reduction before heat treatment in detergent led to two main protein species (Mr 57 000 and 10 500), whereas reduction during or after heat treatment yielded an additional species of Mr 39 000. Heating without any reductive pretreatment yielded the 39 000-Mr form as the major electrophoretic species. Carbohydrate staining showed large amounts of sugar on the 57 000-Mr species and little on the 10 500-Mr form. Significant amounts of haem were associated with this latter subunit. Haem also seemed to be associated with the 57 000-Mr form but not with the 39 000-Mr one. These three subunit forms were isolated and their amino acid composition analysed. The 57 000-Mr and 39 000-Mr forms had very similar amino acid composition and yielded an apparently identical collection of fragments on incubation with CNBr. Once separated, the subunits could not be interconverted. Generally, minor amounts of other molecular-mass forms were observed. The nature of the various molecular-mass forms originating from myeloperoxidase is discussed.

Changes in renal glomerular basement membrane with age and nephritis

1977 ◽  
Vol 55 (12) ◽  
pp. 1197-1206 ◽  
Author(s):  
N. Kalant ◽  
S. Satomi ◽  
R. White ◽  
E. Tel
Keyword(s):  
Amino Acid ◽  
Basement Membrane ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Glomerular Basement Membrane ◽  
Disulfide Bonds ◽  
Sodium Dodecyl ◽  
Collagen Content ◽  
Insoluble Residue ◽  
Adult Rats

Glomerular basement membrane was obtained from normal, young and old adult rats and from animals with antiserum nephritis, daunomycin nephrosis, and lathyrism. With increased age there was an increase in the collagen content of whole glomeruli and of the basement membrane. About 50% of the membrane protein was solubilized in 1% sodium dodecyl sulfate, and a further 35% was solubilized by reduction and alkylation. Inhibition of formation of collagen cross-links by induction of lathyrism did not affect membrane solubility. Preparative disc gel electrophoresis permitted separation of a number of components of different composition; with decreasing molecular weight the collagen content declined from almost 100% to 0%.In antiserum nephritis, there was an increase in the noncollagen components of the membrane and marked alterations in amino acid composition, both of whole membrane and of electrophoretically separated components. In daunomycin nephrosis, the amino acid composition was similar to that of antiserum nephritis. The solubility of membrane from nephritic rats was normal. The composition of the insoluble residue was similar for all membrane preparations and resembled pure collagen. It is suggested that the presence of abnormal noncollagen proteins, associated with the insoluble collagen core by hydrophobic and disulfide bonds, as in antiserum nephritis, is associated with increased membrane permeability leading to proteinuria.

scholarly journals Purification and properties of a proteolytic enzyme from the cercariae of the human trematode parasite Schistosoma mansoni

1982 ◽  
Vol 201 (1) ◽  
pp. 137-144 ◽  
Author(s):  
W J Landsperger ◽  
M A Stirewalt ◽  
M H Dresden
Keyword(s):  
Amino Acid ◽  
Schistosoma Mansoni ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Proteolytic Enzymes ◽  
Sodium Dodecyl ◽  
Skin Penetration ◽  
Cathepsin G ◽  
Trematode Parasite

Skin penetration by the cercarial stage of the human trematode parasite Schistosoma mansoni is mediated by the secretion of proteolytic enzymes able to digest components of mammalian connective tissues. In the present study the purification of these proteinases from cercarial homogenates is reported. The major proteinase species has a mol. wt. of approx. 25 000 and exists in monomeric form as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. This proteinase has an isoelectric point of 6.0. Studies presented here, with a variety of substrates and inhibitors, confirm previous claims that these proteinases belong to the serine class, and, in addition, suggest that they resemble the vertebrate chymotrypsins rather than trypsins or elastases. However, the amino acid composition of the cercarial proteinase differs significantly from bovine chymotrypsin and from the human leucocyte chymotrypsin-like cathepsin G. The amino-acid-composition differences between these proteinases are consistent with their differences in isoelectric point. In order to obtain an insight into the role of the proteinase in skin penetration, its activity on cartilage proteoglycan monomers and on the isolated peptide backbone of proteoglycan was studied. The results of the present study indicate that the cercarial enzyme catalyses a limited specific digestion of the peptide core.

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