Zinc Proteinate Research Articles

Relative bioavailability of organic zinc sources based on tissue zinc and metallothionein in chicks fed conventional dietary zinc concentrations

An experiment was conducted to estimate relative bioavailability (RBV) of Zn in Zinc proteinate and Zinc methionine compared to Zinc acetate as the standard. A total of 432, 1-day-old male broiler chicks was assigned randomly to dietary treatments which included the basal maize–soyabean meal diet (24 mg Zn kg −1 DM) supplemented with 0, 30, 60, or 90 mg kg −1 added Zn as reagent grade Zinc acetate or 30 or 60 mg kg −1 added Zn from Zinc methionine or Zinc proteinate fed for 3, 6, or 9 days. Accumulation of Zn in bone increased ( P<0.001) with supplemental Zn and age. Bone Zn concentration was greater ( P<0.001) in chicks given Zinc proteinate. Hepatic and mucosal metallothionein (MT) increased ( P<0.001) with supplemented Zn and age. Using Zinc acetate as a standard (1.00) in multiple linear regressions gave estimated RBV values of 1.10, 1.24, and 1.16 for Zinc proteinate and 0.88, 0.91 and 0.78 for Zinc methionine at 3, 6, and 9 days, respectively, based on bone Zn concentrations. Similar estimates were calculated using mucosal MT. The coefficient of determination was greater for the mucosal MT regression at 3 days compared to that for bone Zn. Mucosal MT appears to be a suitable criterion to estimate bioavailability of Zn sources during short term trials.

Effect of zinc source (zinc oxide vs zinc proteinate) and level on performance, carcass characteristics, and immune response of growing and finishing steers.

Sixty Angus and Angus x Hereford steers (246 kg initial BW) were used to determine the effects of Zn level and source on performance, immune response, and carcass characteristics of growing and finishing steers. Treatments consisted of 1) control (no supplemental Zn), 2) ZnO, 3) Zn proteinate-A (ZnProt-A, 10% Zn), and 4) ZnProt-B (15% Zn). Treatments 2, 3, and 4 supplied 25 mg of supplemental Zn/kg diet. Steers were individually fed a corn silage-based diet during the 84-d growing phase and a high corn diet during the finishing phase. Cell-mediated and humoral immune response measurements were obtained between d 67 and 74 of the growing phase. Equal number of steers per treatment were slaughtered after receiving the finishing diets for 84 or 112 d. Performance and carcass measurements were similar in steers fed the two ZnProt sources. Zinc supplementation, regardless of source, increased (P < 0.05) ADG during the growing phase. In the finishing phase, ADG (P = 0.10) and gain/feed (P = 0.07) tended to be higher for steers fed ZnProt compared with those supplemented with ZnO. Gain and feed efficiency were similar for control and ZnO-supplemented steers during the finishing phase. Steers fed ZnProt had heavier (P < 0.05) hot carcass weights and slightly higher (P < 0.05) dressing percentages than those in the control or ZnO treatments. Quality grade, yield grade, marbling, and backfat were increased by Zn supplementation, but were not affected by Zn source. In vitro response of lymphocytes to mitogen stimulation and in vivo swelling response following intradermal injection of phytohemagglutinin were not affected by Zn level or source. Humoral immune response following vaccination with infectious bovine rhinotracheitis also was not affected by treatment. Soluble concentrations of Zn in ruminal fluid were higher (P < 0.05) in steers fed ZnProt compared to ZnO steers. Results indicate that ZnProt may improve performance of finishing steers above that observed with inorganic Zn supplementation.

Abstracts

Lack of effect of zinc proteinate on clinical mastitis cell count in dairy cows, Whitaker, D. A., Eayres, K., Aitchison, K. & Kelly, J. M. (1997) Veterinary Journal 153,197Persistence of...

No effect of a dietary zinc proteinate on clinical mastitis, infection rate, recovery rate and somatic cell count in dairy cows

Forty dairy cows, paired at drying off according to expected calving date, milk somatic cell count (SCC) and previous mastitis history, and 10 heifers, paired by date of expected calving, were fed diets in the last 3 weeks of pregnancy which contained either 200 mg zinc proteinate and 60 mg inorganic zinc (Zinc group), or 260 mg inorganic zinc (Control group) per day in addition to the natural content of their feeds. After calving, the Zinc group each received 250 mg zinc proteinate and 140 mg inorganic zinc and the Control group 390 mg inorganic zinc per day above background levels. During the first 100 days of lactation there were no significant differences between the groups in terms of clinical mastitis rates, mastitis caused by environmental organisms, new infection rates or recovery rates. SCC showed no differences between the groups. Monitoring of body condition score and weight change, milk yield, blood metabolite values and fertility showed satisfactory and similar nutrition and productivity in both groups. The trial did not demonstrate any advantages from feeding proteinates to dairy cows and highlights the general absence of published controlled trial data on the subject.

Comparative Net Absorption of Chelated and Inorganic Trace Minerals in Channel Catfish Ictalurus punctatus Diets

AbstractCoefficients of net absorption for copper, iron, manganese, selenium, and zinc were determined for chelated sources (copper proteinate, iron proteinate, manganese proteinate, selenium proteinate, zinc proteinate) and inorganic sources (copper sulfate pentahydrate, ferrous sulfate heptahydrate, manganese sulfate monohydrate, sodium selenite, zinc sulfate hep‐tahydrate) of these elements with channel catfish Ictalurus punctatus. Fish weighing approximately 60 g were placed into 40‐L aquaria (12 fish/aquarium) at a temperature of 28 f 2 C and fed either an egg white‐based, purified diet or a soybean meal‐based, practical diet with and without the test mineral sources for 6 wk then killed and feces collected from the hindgut. Treatments were arranged in a 2 × 2 factorial design. Absorption coefficients for the elements in the basal and mineral supplemented diets were calculated by the indirect indicator (chromic oxide) method and corrected for residual amounts of element in the basal diets. Net absorption of the chelated minerals was significantly higher (p &lt; 0.05) than net absorption of the inorganic minerals in both basal diets. Average percentage improvement in net absorption of chelated minerals over inorganic minerals was 39.3% in the purified diets and 81.1% in the practical diets. These results may indicate that appreciably lower amounts of chelated trace minerals than inorganic trace minerals can be used as supplements in catfish feeds.

Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme

A murine carbonic anhydrase-related protein (CARP) has been expressed in Escherichia coli and purified to near homogeneity. The polypeptide chain consists of 290 amino acid residues and has a calculated molecular mass of 32 950 Da. By introducing two mutations, Arg 117 → His and Glu 115 → Gln, we created a metal-binding center homologous to that in the carbonic anhydrases from the animal kingdom. In contrast to unmodified CARP, this double mutant was isolated as a 1 : 1 zinc-protein complex. While unmodified CARP is catalytically inactive, the mutant catalyzes CO 2 hydration with a significantly higher efficiency than the mammalian low-activity carbonic anhydrase isozyme III. The activity is strongly inhibited by the powerful and selective carbonic anhydrase inhibitor, acetazolamide.

Comparison of chelated zinc and zinc sulfate as zinc sources for growth and bone mineralization of channel catfish ( Ictalurus punctatus) fed practical diets

Zinc methionine (ZnMet), zinc proteinate (ZnPr), and zinc sulfate (ZnSO 4) were evaluated as dietary zinc sources for channel catfish. All diets were practical diets and all known dietary nutrient requirements for channel catfish were satisfied except for zinc. Two experiments were conducted in aquaria in which fish were fed twice daily to approximate satiation for 10 or 12 weeks. In experiment 1, there were no significant differences in weight gain, feed consumption, survival, or bone ash between fish fed ZnSO 4 or ZnMet (15 to 90 mg supplemental zinc kg −1 diet) and fish fed the basal diet (no supplemental zinc, but contained about 50 mg endogenous zinc kg −1). Bone zinc increased linearly as dietary zinc increased for fish fed either ZnSO 4 or ZnMet. Fish fed 90 mg supplemental zinc kg −1 from ZnMet had slightly lower bone zinc than fish fed the same zinc level supplied as ZnSO 4. In experiment 2, no significant differences were observed in weight gain, feed consumption, FCR, and survival of fish fed ZnSO 4 or ZnPr. Bone zinc for fish fed 45 mg supplemental zinc kg −1 from ZnPr was 123.1 μg g −1, compared to 327.4 μg g −1 for fish fed 200 mg supplemental zinc kg −1 from ZnSO 4. Overall, the data indicate that the bioavailabilities of ZnSO 4 and ZnMet to channel catfish are similar when the fish are fed a typical practical diet. The data also demonstrated that 45 mg zinc kg −1 from ZnPr is not equivalent to 200 mg zinc kg −1 from ZnSO 4 to channel catfish as anticipated based on information provided by the manufacturer of ZnPr. In addition, the data show that channel catfish do not need supplemental zinc for maximum growth when fed practical diets containing animal protein, but require supplemental zinc for maximum bone zinc deposition.

Effects of dietary zinc on the assimilation efficiency of carp (Cyprinus cavpio L.)

Adding zinc to the diet of carp lowered assimilation efficiency (AE) proportionately. AE values were higher (and higher proportions of zinc were absorbed) when zinc proteinate replaced zinc sulphate.

Binding of free and protein-associated zinc to rat spermatozoa

1. The zinc content of rat spermatozoa increases, upon ejaculation, from 0.035 to 1.055 μg/10 6 cells. 2. The rat seminal plasma holds zinc both as free ion and as protein-bound forms. 3. Zinc-free ions bind in vitro to rat epididymal spermatozoa. 4. Zinc-protein complexes can be isolated, by a Chromatographic procedure, from the dorsolateral lobe of rat prostate. 5. The isolated zinc-protein complexes bind in vitro to rat epididymal spermatozoa.

Effect of Dietary Calcium Phosphate and Zinc Supplementation on Whole Body Zinc Concentration of Rainbow Trout (Salmo gairdneri)

Groups of rainbow trout (Salmo gairdneri) were fed casein–gelatin diets supplemented with calcium phosphate (Ca3(PO4)2) to produce dietary calcium and phosphorus levels of 1,2, or 4% and 0.9,1.5, or 2.4%, respectively (low, medium, or high calcium phosphate), and supplemented with 20 μg Zn/g diet as ZnSO4, zinc proteinate, or ZnSO4 + EDTA (1000 μg/g). Dietary calcium phosphate levels had no significant effect on weight gain of the fish, although the fish fed the high dietary calcium phosphate level were smaller than the rest. Dietary zinc supplementation had no effect on growth, but significantly increased whole body zinc levels in fish fed diets containing low or medium calcium phosphate. In fish fed diets containing low calcium phosphate, the zinc supplements all increased whole body zinc concentrations. In fish fed diets containing medium calcium phosphate, supplementation with zinc proteinate resulted in higher whole body zinc values than supplementation with other zinc sources. Dietary zinc supplementation did not increase whole body zinc concentrations above control levels in fish fed the experimental diets containing high calcium phosphate. We conclude that increased dietary levels of calcium phosphate reduced whole body zinc concentration of rainbow trout and that 20 μg Zn/g diet was insufficient to overcome this reduction at the highest dietary calcium phosphate level regardless of the form of zinc supplement used.

Identification and determination of copper--and zinc--protein complexes in blood plasma after chromatographic separation on DEAE-Sepharose CL-6B.

Download options Please wait... Article information DOI https://doi.org/10.1039/AN9840900871 Article type Paper Download Citation Analyst, 1984,109, 871-876 BibTex EndNote MEDLINE ProCite ReferenceManager RefWorks RIS Permissions Request permissions Identification and determination of copper-and zinc-protein complexes in blood plasma after chromatographic separation on DEAE-Sepharose CL-6B D. C. Chilvers, J. B. Dawson, M. Bahreyni-Toosi and A. Hodgkinson, Analyst, 1984, 109, 871 DOI: 10.1039/AN9840900871 To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page. If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given. If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page. Read more about how to correctly acknowledge RSC content. Social activity Tweet Share Search articles by author David C. Chilvers John B. Dawson Mohammad-Hossein Bahreyni-Toosi Albert Hodgkinson

High Zinc Supplementation of Rainbow Trout Diets

Abstract Zinc in the form of zinc sulfate or chelated as zinc proteinate was fed in increasing levels (4 to 1,700 µg/g zinc) in an egg-white based diet to fingerling rainbow trout (Salmo gairdneri) to determine potential toxicity. Zinc sulfate was fed for the first 55 days and zinc proteinate for the last 118 days of a 173-day test. Fish fed the lowest level of zinc (4 µg/g zinc, a zinc-deficient diet) had poor growth and high mortalities, while the lowest level of added zinc (90 µg/g) reduced mortalities and markedly improved growth. Higher levels of supplemented zinc, up to 1,700 µg/g, had no further effect on growth or survival. Zinc concentration in liver, blood, and gills increased with dietary levels of zinc above 90 µg/g. Trout showed no signs of zinc toxicity during feeding with levels of dietary zinc as high as 1,700 µg/g.

Kinetics of metal dissociation in the yeast Cu2,Zn2-superoxide dismutase. Apparent asymmetry in the metal binding sites

The inactivation and metal depletion of the yeast Cu2, Zn2-superoxide dismutase have been examined in the presence of a number of chelating reagents. Total inactivation and metal depletion occurred only at pH ≤3.5. The loss of enzyme activity exhibited biphasic kinetics and was directly related to the rate of loss of copper from the protein. Two rate constants characterized also the dissociation of zinc from the native enzyme. At low pH, in the absence of chelating reagents, there is a fifty percent reduction in dismutase activity and a concommitant decrease in the metal concentration to one equivalent each of copper and zinc per mole dimer. It is apparent that the dissociation constants for the copper-protein and zinc-protein complexes differ between the subunits of the dimeric enzyme. Comparison of the hydrodymanic and optical properties of the native and apo-SOD reveals changes in the structure and stability of the protein as a result of metal removal.

Characterization of jack-bean alpha-D-mannosidase as a zinc metalloenzyme.

1. Two methods were used to obtain alpha-mannosidase free from unbound Zn2+, (a) by removal of excess of metal ion from preparations purified in the presence of Zn2+ and (b) by purification under conditions that eliminate the need to add Zn2+. 2. The purified enzyme is homogeneous on ultracentrifugation, polyacrylamide-gel electrophoresis and gel chromatography. 3. The molecular weight is estimated to be 230 000. 4. The enzyme contains between 470 and 565 mug of zinc/g of protein, corresponding to between 1.7 and 2 atoms of zinc/enzyme molecule. The contents of other metals are much lower. 5. The enzyme is inactivated by chelating agents and activity is restored by Zn2+. 6. No other metal ion was found to replace Zn2+ with retention of activity. Some bivalent metal ions, e.g. Cu2+, rapidly inactivate the enzyme. 7. The results indicate that jack-bean alpha-mannosidase exists naturally as a zinc-protein complex and may be considered as a metalloenzyme.

Determination of zinc distribution between albumin and α2-macroglobulin in human serum

Addition of an equal volume of 20% ( w w ) polyethylene glycol 6000 to human serum leads to separation of two major zinc ligands. α 2-Macroglobulin, a zinc metalloprotein, is precipitated, while albumin, which forms a zinc-protein complex in serum, remains soluble. Total serum zinc and albumin-bound zinc are measured; α 2-macroglobulin bound zinc is obtained by difference. The following values of zinc distribution were obtained in a study of 16 normal males; serum zinc, 82 ± 9 (mean ± standard deviation) μg/100 ml; albumin-bound zinc 66 ± 7 μg/100 ml and α 2-macroglobulin-bound zinc 16 ± 3 μg/100 ml.

Binding of EDTA, Histidine and Acetylsalicylic Acid to Zinc–Protein Complex in Intestinal Content, Intestinal Mucosa and Blood Plasma

ETHYLENEDIAMINETETRAACETIC acid (EDTA) added to a diet containing isolated soybean protein has improved the growth rate and reduced the incidence of a hock disorder caused by zinc deficiency1 in chickens. Furthermore, the addition of histidine and 8 ml. anti-arthritic agents, including acetylsalicylic acid (aspirin), prevented “arthritic-like” leg abnormalities in chickens fed such diets deficient in zinc2,3. Supplementation of the diet with zinc promoted normal growth and feather development, and prevented leg abnormalities, while supplementation with the anti-arthritic agents had little or no effect on the symptoms of zinc deficiency except the leg defect. Amino-acids, particularly histidine, seem to be involved in the passage of zinc from the intestinal lumen to the blood stream4,5. EDTA was found to bind zinc in the intestinal digesta and seemed to remain bound as it passed through the intestinal mucosa and was transported in the blood plasma, confirming previous work5. We have investigated the binding of histidine and aspirin to zinc and their transport from intestinal digesta to the blood stream to find out whether these compounds alleviate the abnormal leg conditions by the same mechanism.

Alpha-mannosidase as a zinc-dependent enzyme.

CADMIUM has been reported to have a teratogenic effect in the golden hamster1, which is reversed by zinc. This prompts us to draw attention to our recent observation2 that zinc is an essential component of α-mannosidase. The active zinc–protein complex is readily dissociable at pH 5, the pH of optimum enzyme activity and the zinc ion can be displaced by cadmium, cobalt and other bivalent ions, with almost complete loss of enzyme activity (Fig. 1). These observations apply equally to the enzyme from rat epididymis3,4, jack bean meal5 and the limpet, Patella vulgata6.

Bacillus subtilis α-amylase, a zinc-protein complex

1. 1. Crystalline Bacillus subtilis α-amylase, which has been reported to be a calcium metalloenzyme, also contains small amounts of zinc. Under normal conditions, this enzyme exists in the form of a dimer. 2. 2. Dissociation of the dimer takes place in the presence of metal-binding agents whereas dimerization is induced by zinc ions. One atom of zinc per molecule of dimer is taken up by the protein during dimerization and released as dissociation proceeds according to the following scheme: [Prot—Ca x—Zn—[Prot—Ca x] ▪2[Prot—Ca x]+Zn 3. 3. Formation of this zinc-protein complex appears to be peculiar to B. subtilis α-amylase. Intermolecular cross-linking under the influence of zinc has not been observed with α-amylases from human saliva, hog pancreas, or Aspergillus oryzae. 4. 4. Calcium ions do not induce dimerization of bacterial amylase.