scholarly journals Effect of zinc injection on Zn binding in cytosols of several tissues of kids

1980 ◽  
Vol 44 (3) ◽  
pp. 355-360 ◽  
Author(s):  
S. Tanabe

1. An experiment was conducted with goat kids to determine the effect of zinc injection on Zn binding in cytosols of several tissues of kids.2. Following the Zn load, plasma Zn increased for 8 h then decreased. Zn injection significantly increased the Zn contents of the liver and kidney.3. Injection of Zn into kids stimulated the production of Zn in a fraction with an apparent molecular weight of approximately 10000 in the cytosols of the liver, kidney and small intestinal mucosa. It is suggested that these fractions probably correspond to metallothioneins, Rumen papilla did not synthesize Zn-containing protein in response to an acute administration of Zn.4. Zn injection significantly decreased the Cu content of the liver and affected the distribution of Cu in hepatic cytosol fraction, suggesting an interaction between these two elements.5. The volume of bile collected in the gall bladder and its Zn content were markedly increased by Zn injection, suggesting that bile is one of the Zn excretion routes in kids.

1981 ◽  
Vol 197 (1) ◽  
pp. 55-65 ◽  
Author(s):  
M Davie

Ca2+-binding activity was investigated in human small-intestinal mucosal cytosol. Binding was detected in fractions with molecular weights of 28000 and about 900000, as determined by gel filtration. No binding was found at molecular weight 12000-13000 (the molecular weight of calcium-binding protein in lower mammalian species) until the cytosol had been subjected to a hollow-fibre-filtration step. The appearance of Ca2+-binding at molecular weight 12000-13000 was associated with a decline in the 28000-mol.wt. calcium-binding fraction. The 12000-13000-mol.wt. fraction contained two distinct calcium-binding proteins. One of these proteins had properties similar to those of pig calcium-binding protein. Antiserum to this protein reacted against the 28000-mol.wt calcium-binding fraction in cytosol from human small-intestinal mucosa and from human kidney. An immunoassay method for one of the calcium-binding proteins was established. In normal duodenal mucosa the concentration was 915 micrograms/g and in the ileum it was 443 micrograms/g of mucosa. A subject with hypercalcaemic sarcoidosis had 1200 micrograms/g of mucosa in the jejunum, and a subject with an undetectable concentration of plasma 25-hydroxycholecalciferol had concentrations of calcium-binding protein in the mucosa similar to those found in normal subjects.


1973 ◽  
Vol 135 (4) ◽  
pp. 609-615 ◽  
Author(s):  
Manjusri Das ◽  
A. N. Radhakrishnan

1. A highly active and electrophoretically homogeneous dipeptidase was purified from the soluble extracts of monkey small-intestinal mucosa. 2. By gel-filtration studies the molecular weight of the enzyme was found to be 107000. It is composed of two identical, subunits of molecular weight 54000. 3. A paper-chromatographic method of dipeptidase assay was developed to overcome some of the difficulties encountered in the generally used spectrophotometric procedure. By using this method, the Km and k0 values of a few substrates were determined. 4. The substrate specificity of the enzyme was investigated in great detail with substrates of a wide range of possible structural types. The enzyme hydrolyses a very large proportion of the range of dipeptides tested. This enzyme, which exhibits such a wide range of action, has been termed the ‘master’ dipeptidase of the intestine. Glycylglycine, glycyl-l-proline, glycyl-l-histidine, l-prolylglycine and some of the arginine- and aspartic acid-containing dipeptides were not substrates and are possibly hydrolysed by other peptidases. These results therefore suggest that in the intestine the number of dipeptidases is rather limited. 5. In the light of these findings, the implications on the role of dipeptidases in intestinal peptide transport are discussed.


1975 ◽  
Vol 47 (6) ◽  
pp. 469-479
Author(s):  
Ruth Stabel-Taucher ◽  
Esko Nurmi ◽  
Eeva Karppanen

A total of 120 normal slaughter cows were analyzed with respect to Cu, Zn, Pb, Cd and Hg in muscle, liver and kidney. The cows orginated from 6 different slaughter-houses throughout the country. Imported cow livers, represented by 10 samples from Australia, 10 from Poland and 15 from Ireland, were also analyzed for comparison with the Finnish material. The Cu content in the Finnish animals turned out to be relatively low. The imported samples had even lower contents. There seemed to be no correlation between the Cu contents in muscle, liver and kidney. Statistical tests established that the mean Cu content in livers from Oulu was significantly higher than most of the others at the 5 % level. The Zn determinations revealed the highest amounts in the muscle. No correlation between the contents in muscle, liver and kidney was shown. The animals from Seinäjoki had the highest Zn contents, significantly different from most of the others. The imported livers did not differ much from the domestic ones as regards Zn content. The same was true for the Pb content. The correlation coefficients of Pb in muscle, liver and kidney were low. The animals from Kouvola contained the highest amounts of Pb, and the mean Pb content of these animals’ kidneys was significantly different from all the others. The Cd content was highest in the animals from Turku. A good correlation was observed between the Cd contents in liver and kidney. The Cd content of the imported livers was of the same order as that of the Finnish ones. No correlation was found between the Zn, Pb and Cd contents. The amounts of Hg in Finnish cattle were very low, especially so in animals from the North of Finland. The Hg content of the imported samples was of the same order as the figures recorded from the South of Finland.


1980 ◽  
Vol 59 (s6) ◽  
pp. 25s-27s ◽  
Author(s):  
K. Yamamoto ◽  
F. Ikemoto ◽  
M. Kawamura ◽  
K. Takaori

1. The low-molecular-weight (40 000) form of renin was converted into the high-molecular-weight (60 000) form of renin with sulphydryl oxidation, and the high-molecular-weight form of renin was re-converted into the low-molecular-weight form with a reduction of disulphide bonds in the renal cortical homogenate of the dog. Therefore, the low- and high-molecular-weight forms of renin were interconvertible. 2. The formation of high-molecular-weight form of renin required a renin binding substance which was found to be included in the cytosol fraction of kidney cortex of the dog. 3. The renin binding substance of the dog was unstable to heat and low pH, but vitally resistant to Triton X-100 and chloroform. It did not bind to concanavalin A Sepharose 4B. 4. The renin binding substance was eluted in the molecular-weight region between 156 000 and 60 000 on Sephadex G-200, and such apparent molecular weight was not altered by urea at 4 mol/l; thus molecular weight greater than the theoretically expected value of 20 000 was indicated.


1983 ◽  
Vol 36 (6) ◽  
pp. 475 ◽  
Author(s):  
NJ Benevenga ◽  
BC Radcliffe ◽  
AR Egan

The rate of oxidization of the carboxyl and methyl carbons of (I4C]methionine to CO2 by homogenates of liver, kidney cortex, pancreas, muscle and small intestinal mucosa was studied in two breeds of sheep (Merino and Poll Dorset Horn) at three ages (2 weeks, 3 months, 4 years). Sodium a-keto-,),methiolbutyrate (0�4 mM) stimulated production of CO2 from the carboxyl carbon of methionine, but not from the methyl carbon. Sodium pyruvate did not affect the recovery of CO2 from either carboxyl or methyl of methionine. Sodium formate (15 mM) suppressed the conversion of the methyl carbon of methionine to CO2 by liver and kidney homogenates to 4 and 50%, respectively, of control values, but did not affect the percentage of carboxyl carbon of methionine recovered in CO2 with either tissue. With addition of S-methyl-L-cysteine (40 mM) and 3-methylthiopropionate (10 mM) the percentage of methyl and carboxyl carbons recovered in CO2 was reduced to about 20% of control values in homogenates of both tissues.


1990 ◽  
Vol 63 (03) ◽  
pp. 499-504 ◽  
Author(s):  
A Electricwala ◽  
L Irons ◽  
R Wait ◽  
R J G Carr ◽  
R J Ling ◽  
...  

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)


1975 ◽  
Vol 33 (03) ◽  
pp. 553-563 ◽  
Author(s):  
B Østerud ◽  
K Laake ◽  
H Prydz

SummaryThe activation of factor IX purified from human plasma has been studied. Factor XIa and kallikrein separately activated factor IX to factor IXa. In both cases factor IX a had an apparent molecular weight of about 42–45000 in sodium dodecyl sul-phate-polyacrylamide disc gel electrophoresis compared with a molecular weight of about 70000 for the native factor IX. The activation by XIa required Ca2+-ions whereas Ca2+-ions did not influence the activation by kallikrein. A mixture of tissue thromboplastin and factor VII or RusselPs-viper venom alone did not activate factor IX. Trypsin activated and plasmin inactivated factor IX.


2009 ◽  
Vol 102 (9) ◽  
pp. 1285-1296 ◽  
Author(s):  
Maud Le Gall ◽  
Mélanie Gallois ◽  
Bernard Sève ◽  
Isabelle Louveau ◽  
Jens J. Holst ◽  
...  

Sodium butyrate (SB) provided orally favours body growth and maturation of the gastrointestinal tract (GIT) in milk-fed pigs. In weaned pigs, conflicting results have been obtained. Therefore, we hypothesised that the effects of SB (3 g/kg DM intake) depend on the period (before v. after weaning) of its oral administration. From the age of 5 d, thirty-two pigs, blocked in quadruplicates within litters, were assigned to one of four treatments: no SB (control), SB before (for 24 d), or after (for 11–12 d) weaning and SB before and after weaning (for 35–36 d). Growth performance, feed intake and various end-point indices of GIT anatomy and physiology were investigated at slaughter. The pigs supplemented with SB before weaning grew faster after weaning than the controls (P < 0·05). The feed intake was higher in pigs supplemented with SB before or after weaning (P < 0·05). SB provided before weaning improved post-weaning faecal digestibility (P < 0·05) while SB after weaning decreased ileal and faecal digestibilities (P < 0·05). Gastric digesta retention was higher when SB was provided before weaning (P < 0·05). Post-weaning administration of SB decreased the activity of three pancreatic enzymes and five intestinal enzymes (P < 0·05). IL-18 gene expression tended to be lower in the mid-jejunum in SB-supplemented pigs. The small-intestinal mucosa was thinner and jejunal villous height lower in all SB groups (P < 0·05). In conclusion, the pre-weaning SB supplementation was the most efficient to stimulate body growth and feed intake after weaning, by reducing gastric emptying and intestinal mucosa weight and by increasing feed digestibility.


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