TRIENNIAL LACTATION SYMPOSIUM: Mammary metabolism of amino acids in dairy cows1,2

1. The following techniques, which have been applied successfully to goats, were used to study mammary metabolism in lactating sows:(I) measurements of mammary arteriovenous (A-V) differences in milk precursors in the conscious undisturbed animal (five sows); (2) continuous intravenous infusion of [U-14C]glucose with concomitant arterial and mammary venous blood sampling for measurement of mammary blood flow and specific radioactivity of glucose and CO, (one sow); (3) perfusion of the isolated gland in vitro (eight glands from four sows), with the inclusion of [U-14C]glucose (two glands) and [U-14C]acetate(two glands) in the substrate mixture.2. Sow mammary tissue was similar to that goats in its milk yield, blood flow, and glucose uptake per unit weight of tissue. As in goats, mammary uptake of glucose was many times that of the rest of the body and the total mammary tissue was utilizing about half of the total glucose entering the circulation. Glucose was a major source of milk lactose and glycerol and of mammary CO2.3. Of the plasma lipid components, only the triglyceride fraction was consistently and significantly removed by the gland. In contrast to the results obtained for the goat, both [U-14C[acetate and [U-14C]glucose carbon were used for milk fatty acid synthesis, and although the pattern of labelling of fatty acid from each precursor was similar, the formation of fatty acids from glucose was at least five times greater than that from acetate. Quantitative evaluation of the contribution of these precursors was not possible, but the RQ (1.09–1.63) suggest that in some instances it may have been considerable.4. The substantial A-V differences of most plasma essential amino acids suggest that these are the sole precursors of the corresponding residues in the mammary synthesized protein. The low A-V differences for several non-essential amino acids suggest that these are synthe- sized in the gland; this suggestion is supported by the incorporation of glucose carbon into non-essential amino acid residues of casein observed in one experiment. However, in contrast to results with the goat, mammary absorption of serine was consistently large.

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Effects of graded levels of duodenal infusions of leucine on mammary uptake and output in lactating dairy cows

Journal of Dairy Research ◽

10.1017/s0022029906001841 ◽

2006 ◽

Vol 73 (3) ◽

pp. 328-339 ◽

Cited By ~ 29

Author(s):

Henri Rulquin ◽

Pawel M Pisulewski

Keyword(s):

Amino Acids ◽

Milk Fat ◽

Milk Protein ◽

Latin Square ◽

Essential Amino Acids ◽

Lactating Dairy Cows ◽

Milk Output ◽

Milk Protein Content ◽

Output Ratio ◽

Mammary Metabolism

Four multiparous Holstein cows, each equipped with a duodenal cannula and an ultrasonic mammary blood flow probe, were assigned to a 4×4 Latin square to measure the effects of duodenal infusions of Leu (0, 40, 80 and 120 g/d) on lactational responses and mammary metabolism of nutrients. Cows were fed a diet of 67·0% corn silage, 5·3% grass hay, 14·2% peas, 7·8% maize starch, 1·0% each of molasses, urea, and sodium bicarbonate and 2·4% minerals and vitamins. Requirements of the remaining 9 essential amino acids were met by infusing into the duodenum 323 g/d of a mixture of amino acids including, Ile, Val, Met, Lys, Trp, Phe, His, Thr, Arg, Tyr and Glu. Milk protein content and yield were highest with 40 g/d of Leu and then progressively declined. Milk fat content and yield were significantly decreased over the entire range of Leu infusions. Arterial concentrations of Leu increased linearly and corresponding mammary arterio-venous differences increased to a plateau with 80 g/d of Leu. As Leu infusions increased, extraction rates of Leu decreased linearly, whereas those of Ile, Val, Lys, Arg, Thr and Tyr were significantly increased. Leu was taken up by the mammary gland according to milk output with 0 and 40 g/d of Leu infused and then largely in excess. Based on responses of protein yield and mammary uptake to milk output ratio, Leu concentration in total amino acids absorbed in the small intestine needs to be close to 8·9% for optimal milk protein synthesis.

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Homochirality as the Signature of Extra-Terrestrial Life

International Astronomical Union Colloquium ◽

10.1017/s0252921100015037 ◽

1997 ◽

Vol 161 ◽

pp. 505-510

Author(s):

Alexandra J. MacDermott ◽

Laurence D. Barron ◽

Andrè Brack ◽

Thomas Buhse ◽

John R. Cronin ◽

...

Keyword(s):

Amino Acids ◽

Protein Synthesis ◽

Optical Rotation ◽

Physical Origin ◽

Natural Choice ◽

Rosetta Mission ◽

Terrestrial Life ◽

Subsurface Layers ◽

Solar System Bodies ◽

Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

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Hydrogen Cyanide Polymers from the Impact of Comet P/Shoemaker-Levy 9 on Jupiter

International Astronomical Union Colloquium ◽

10.1017/s025292110001469x ◽

1997 ◽

Vol 161 ◽

pp. 179-187

Author(s):

Clifford N. Matthews ◽

Rose A. Pesce-Rodriguez ◽

Shirley A. Liebman

Keyword(s):

Amino Acids ◽

Solar System ◽

Hydrogen Cyanide ◽

Nitrogen Heterocycles ◽

Laboratory Studies ◽

Heterogeneous Solids ◽

The Many ◽

Comet Halley ◽

The Impact ◽

By Products

AbstractHydrogen cyanide polymers – heterogeneous solids ranging in color from yellow to orange to brown to black – may be among the organic macromolecules most readily formed within the Solar System. The non-volatile black crust of comet Halley, for example, as well as the extensive orangebrown streaks in the atmosphere of Jupiter, might consist largely of such polymers synthesized from HCN formed by photolysis of methane and ammonia, the color observed depending on the concentration of HCN involved. Laboratory studies of these ubiquitous compounds point to the presence of polyamidine structures synthesized directly from hydrogen cyanide. These would be converted by water to polypeptides which can be further hydrolyzed to α-amino acids. Black polymers and multimers with conjugated ladder structures derived from HCN could also be formed and might well be the source of the many nitrogen heterocycles, adenine included, observed after pyrolysis. The dark brown color arising from the impacts of comet P/Shoemaker-Levy 9 on Jupiter might therefore be mainly caused by the presence of HCN polymers, whether originally present, deposited by the impactor or synthesized directly from HCN. Spectroscopic detection of these predicted macromolecules and their hydrolytic and pyrolytic by-products would strengthen significantly the hypothesis that cyanide polymerization is a preferred pathway for prebiotic and extraterrestrial chemistry.

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Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

1982 ◽

Vol 40 ◽

pp. 294-295

Author(s):

E.M. Kuhn ◽

K.D. Marenus ◽

M. Beer

Keyword(s):

Amino Acids ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Electron Microscopic ◽

Good Correspondence ◽

Specific Staining ◽

Type Iii ◽

Different Types ◽

Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

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Prevalence of the pit and antipit in the genus Glycine

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100129218 ◽

1987 ◽

Vol 45 ◽

pp. 986-987

Author(s):

R. W. Yaklich ◽

E. L. Vigil ◽

W. P. Wergin

Keyword(s):

Amino Acids ◽

Endoplasmic Reticulum ◽

Glycine Max ◽

Seed Coat ◽

Cell Types ◽

Abaxial Surface ◽

Legume Seed ◽

Initial Report ◽

Cone Cells ◽

Glycine Max L

The legume seed coat is the site of sucrose unloading and the metabolism of imported ureides and synthesis of amino acids for the developing embryo. The cell types directly responsible for these functions in the seed coat are not known. We recently described a convex layer of tissue on the inside surface of the soybean (Glycine max L. Merr.) seed coat that was termed “antipit” because it was in direct opposition to the concave pit on the abaxial surface of the cotyledon. Cone cells of the antipit contained numerous hypertrophied Golgi apparatus and laminated rough endoplasmic reticulum common to actively secreting cells. The initial report by Dzikowski (1936) described the morphology of the pit and antipit in G. max and found these structures in only 68 of the 169 seed accessions examined.

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Imaging polymers, proteins and dna in aqueous solutions with the atomic force microscope

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100152136 ◽

1989 ◽

Vol 47 ◽

pp. 32-33

Author(s):

S.A.C. Gould ◽

B. Drake ◽

C.B. Prater ◽

A.L. Weisenhorn ◽

S.M. Lindsay ◽

...

Keyword(s):

Amino Acids ◽

Dna Sequencing ◽

Aqueous Solutions ◽

Atomic Force Microscope ◽

Piezoelectric Crystal ◽

Atomic Force ◽

Structure Of Molecules ◽

Optical Lever

The atomic force microscope (AFM) is an instrument that can be used to image many samples of interest in biology and medicine. Images of polymerized amino acids, polyalanine and polyphenylalanine demonstrate the potential of the AFM for revealing the structure of molecules. Images of the protein fibrinogen which agree with TEM images demonstrate that the AFM can provide topographical data on larger molecules. Finally, images of DNA suggest the AFM may soon provide an easier and faster technique for DNA sequencing.The AFM consists of a microfabricated SiO2 triangular shaped cantilever with a diamond tip affixed at the elbow to act as a probe. The sample is mounted on a electronically driven piezoelectric crystal. It is then placed in contact with the tip and scanned. The topography of the surface causes minute deflections in the 100 μm long cantilever which are detected using an optical lever.

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