Three or two times daily milking of older cows and first lactation cows for entire lactations. Dils, R. Milk fat synthesis. Comparative aspects of milk fat synthesis. Dunkley, W. Smith, and A. Effects of feeding protected tallow on composition of milk and milk fat. Eigel, W. Butler, C. Ernstrom, H. Farrell, Jr, V. Harwalker, R. Jenness, and R. Nomenclature of proteins of cow's milk: Fifth revision. Emery, R. Feeding for increased milk protein. Eppard, P. Bauman, J. Bitman, D.
Wood, R. Akers, and W. Effect of dose of bovine growth hormone on milk composition Alpha-lactalbumin, fatty acids, and mineral elements. Faulkner, A, and M. Secretion of citrate into milk. Dairy Res. Fernando, R. Spahr, and E. Comparison of electrical conductivity of milk with other indirect methods for detection of subclinical mastitis. Fettman, M J, L. Chase, J. Bentinck-Smith, C. Coppock, and S. Nutritional chloride deficiency in early lactation Holstein cows. Fogerty, A.
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Influence of nutritional factors on the yield and content of milk fat: Protected polyunsaturated fat in the diet. Dairy Fed. Forar, F. Kincaid, R. Preston, and J. Variation of inorganic phosphate in blood plasma and milk lactating cows. Forester, R. Grieve, J. Buchanan-Smith, and G. Effect of dietary protein degradability on cows in early lactation. Franke, A. Bruhn, and R. Factors affecting iodine concentration of milk of individual cows. Gaunt, S. Genetic and environmental changes in milk consumption. Genetic variation in the yields and contents of milk constituents.
Gisi, D. DePeters, and C. Three times daily milking of cows in California dairy herds. Grappin, R. Packard, and R. Variability and interrelationship of various herd milk components. Food Prot. Hansen, W. Otterby, J. Donker, R.
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Lundquist, and J. Influence of grain concentrations, forage type, and methionine hydroxy analog on lactational performance of dairy cattle. Henderson, S. Amos, and J. Influence of dietary crude protein concentration and degradability on milk production, composition, and ruminal protein metabolism. Holter, J. Urban, Jr. Hayes, and H.
Utilization of diet components fed blended or separately to lactating cows. Hylton, and C. Varying protein content and nitrogen solubility for pluriparious, lactating Holstein cows: Lactation performance and profitability. Iyengar, G. Vienna: International Atomic Energy Agency. Jenkins, T. Effect of fatty acids of calcium soaps on rumen and total nutrient digestibility of dairy rations.
Disorders of Acid-Base Balance – Anatomy and Physiology
Jenness, R. Biochemical and nutritional aspects of milk and colostrum. Larson, editor. Ames: Iowa State University Press. Kaufman, W. Protein degradation and synthesis within the reticulorumen in relation to milk protein synthesis. Kawas, J. Jorgensen, A. Hardie, and J. Change in feeding value of alfalfa hay with stage of maturity and concentrate level.
Keown, J. Everett, N. Empet, and L. Lactation curves. Kitchen, B. Bovine mastitis: Milk compositional changes and related diagnostic tests. Kroeker, E. Ng-Kwai-Hang, J. Hayes, and J. Effect of beta-lactoglobulin variant and environmental factors on variation in the detailed composition of bovine milk serum proteins. Kuhn, N.
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The biosynthesis of lactose. Kung, L. Performance of high producing cows in early lactation fed protein of varying amounts, sources, and degradability. Knzdzal-Savoie, S. Manson, and J. The constituents of cow's milk. Larson, B. Biosynthesis and secretion of milk protein: A review. Biosynthesis and cellular secretion of milk. Larson, L. Wallen, F. Owen, and S. Relation of age, season, production and heath indices to iodine and beta-carotene concentrations in cow's milk.
Linn, J. The addition of fats to diets of lactating dairy cows: A review. Redwood Falls, Minn. Feeding strategies in dairy nutrition. Paul, Minn. Lundquist, R. Linn, and D. Influence of dietary, energy and protein on yield and composition of milk from cows fed methionine hydroxy analog. E Otterby, and J. Influence of formaldehyde-treated soybean meal on milk production. Dairy, Sci. Madsen, J. The effect of formaldehyde-treated protein and urea on milk yield and composition in dairy cows. Acta Agric. Marshall, S. Complete rations for dairy cattle. Methods of preparation and roughage-to-concentrate ratios of blended rations with corn silage.
Mepham, T. Amino acid utilization by lactating mammary gland. Mercier, J. Milk protein synthesis. Mertens, D. Effect of fiber on feed quality for dairy cows. Milam, K. Coppock, J. West, J. Lanham, D. Nave, J. Labore, R. Stermer, and C.
Effects of drinking water temperature on production responses m lactating Holstein cows in summer. Needs, E. Lipid composition of milk from cows with experimentally induced mastitis. Ng-Kwai-Hang, K. Hayes, J. Moxley, and H. Environmental influences on protein content and composition of bovine milk.
Percentages of protein and nonprotein nitrogen with varying fat and somatic cells in bovine milk. Oldham, J. Amino acid metabolism in ruminants. Ithaca, N. Oltner, R. Emanuelson, and H. Urea concentrations in milk in relation to milk yield, live weight, lactation number and amount and composition of feed given to dairy cows. Livestock Prod. Owen, J. Complete-diet feeding of dairy cows. Haresign, editor; and D. Cole, editor. London: Butterworth. Palmquist, D. Fat in lactation rations: Review. Peaker, M. Soluble milk constituents.
Protein Buffers in Blood Plasma and Cells
Peel, C. Sandles, K. Quelch, and A. The effects of long-term administration of bovine growth hormone on the lactational performance of identical-twin dairy cows. Poutrel, B. Caffin, and P. Physiological and pathological factors influencing bovine serum albumin content in milk.
Rogers, G. The effects of some nutritional and nonnutritional factors on milk protein concentration and yield.
Dairy Technol. Rolleri, G. Larson, and R. Protein production in the bovine. Breed and individual variations in the specific protein constituents of milk. Rook, J. Principles involved in manipulating the yields and concentrations of constituents in milk. Schingoethe, D. Whey utilization in animal feeding: A summary and evaluation. Schneider, P. Beede, and C. Responses of lactating cows to dietary sodium source and quantity and potassium quantity during heat stress.
Schultz, L. Somatic cell in milk—physiological aspects and relationship to amount and composition of milk. Schwab, C. Satter, and A. Response of lactating cows to abomasal infusions of amino acids. Shaver, R. Nytes, L. Satter, and N. Influence of amount of feed intake and forage physical form on digestion and passage of prebloom alfalfa hay in dairy cows.
Storry, J. Influence of nutritional factors on the yield and content of milk: Nonprotected fat in the diet. Influence of nutritional factors on yield and content of milk: Protected nonpolyunsaturated fat in the diet. Sutton, J. Influence of nutritional factors on the yield and content of milk fat: Dietary components other than fat.
Sutton J. Digestion and absorption of energy substrates in the lactating cow. Tallamy, P. Influence of mastitis on properties of milk. Total and free concentrations of major minerals in skim milk. Thomas, P. Influence of nutrition on the yield and content of protein in milk. Dietary protein and energy supply. Milk protein. Manipulation of milk composition to meet market needs. Tucker, H. Endocrine and neural control of the mammary gland. Van Vleck, L. Breeding for increased milk protein. Wheelock, J. Influence of physiological factors on the yields and contents of milk constituents.
Wilcox, C. Genetic considerations of economic importance: Milk yield, composition and quality. Wilcox, editor; , H. Van Horn, editor; , B. Harris, Jr. Head, editor; , S. Marshall, editor; , W. Thatcher, editor; , D. Webb, editor; , and J. It occurs when the blood is too alkaline pH above 7. A transient excess of bicarbonate in the blood can follow ingestion of excessive amounts of bicarbonate, citrate, or antacids for conditions such as stomach acid reflux—known as heartburn.
The oversecretion of ACTH results in elevated aldosterone levels and an increased loss of potassium by urinary excretion. Other causes of metabolic alkalosis include the loss of hydrochloric acid from the stomach through vomiting, potassium depletion due to the use of diuretics for hypertension, and the excessive use of laxatives. Respiratory acidosis occurs when the blood is overly acidic due to an excess of carbonic acid, resulting from too much CO 2 in the blood. Respiratory acidosis can result from anything that interferes with respiration, such as pneumonia, emphysema, or congestive heart failure.
Respiratory alkalosis occurs when the blood is overly alkaline due to a deficiency in carbonic acid and CO 2 levels in the blood. This condition usually occurs when too much CO 2 is exhaled from the lungs, as occurs in hyperventilation, which is breathing that is deeper or more frequent than normal. An elevated respiratory rate leading to hyperventilation can be due to extreme emotional upset or fear, fever, infections, hypoxia, or abnormally high levels of catecholamines, such as epinephrine and norepinephrine.
Surprisingly, aspirin overdose—salicylate toxicity—can result in respiratory alkalosis as the body tries to compensate for initial acidosis. Watch this video to see a demonstration of the effect altitude has on blood pH. What effect does high altitude have on blood pH, and why? Various compensatory mechanisms exist to maintain blood pH within a narrow range, including buffers, respiration, and renal mechanisms. Although compensatory mechanisms usually work very well, when one of these mechanisms is not working properly like kidney failure or respiratory disease , they have their limits.
If the pH and bicarbonate to carbonic acid ratio are changed too drastically, the body may not be able to compensate. Moreover, extreme changes in pH can denature proteins. Extensive damage to proteins in this way can result in disruption of normal metabolic processes, serious tissue damage, and ultimately death. Respiratory compensation for metabolic acidosis increases the respiratory rate to drive off CO 2 and readjust the bicarbonate to carbonic acid ratio to the level.
Gout: Risk Factors, Diagnosis and Treatment
This adjustment can occur within minutes. Respiratory compensation for metabolic alkalosis is not as adept as its compensation for acidosis. The normal response of the respiratory system to elevated pH is to increase the amount of CO 2 in the blood by decreasing the respiratory rate to conserve CO 2. There is a limit to the decrease in respiration, however, that the body can tolerate. Hence, the respiratory route is less efficient at compensating for metabolic alkalosis than for acidosis. Metabolic and renal compensation for respiratory diseases that can create acidosis revolves around the conservation of bicarbonate ions.
These processes increase the concentration of bicarbonate in the blood, reestablishing the proper relative concentrations of bicarbonate and carbonic acid. Lab tests for pH, CO 2 partial pressure pCO 2 ,and HCO 3 — can identify acidosis and alkalosis, indicating whether the imbalance is respiratory or metabolic, and the extent to which compensatory mechanisms are working. The blood pH value, as shown in Table 3 , indicates whether the blood is in acidosis, the normal range, or alkalosis. The pCO 2 and total HCO 3 — values aid in determining whether the condition is metabolic or respiratory, and whether the patient has been able to compensate for the problem.
The large hydrogen-ion load generated during their pathologic production, in diabetic ketoacidosis, for example, rapidly overwhelms the normal buffering capacity and leads to a metabolic acidosis with an increased anion gap . Ketolysis is the process by which ketone bodies produced in the liver are converted in non-liver tissues , into acetyl CoA which, on complete oxidation via the tricarboxylic acid cycle and oxidative phosphorylation , provides energy for various intracellular metabolic activities Figure 3.
Ketolysis occurs in the mitochondria of many extrahepatic organs. The central nervous system is particularly dependent on the delivery of ketone bodies produced in the liver for the process of ketolysis, since ketogenesis occurs very slowly if at all in the central nervous system . The acetone is formed by non-enzymic decarboxylation of acetoacetate and cannot be used as an energy source. Acetoacetate and 3-hydroxybutyrate pass from the liver to the general circulation and are absorbed by non-hepatic tissues where they can be used as fuel.
The 3-hydroxybutyrate is oxidized to acetoacetate by 3 hydroxy butyrate dehydrogenase denoted as I in the figure and then converted to acetoacetyl CoA by acetoacetyl succinyl CoA transferase II. Based on slide 25 in Chaudhuri . Interplay between ketone body production ketogenesis in the liver and ketone body utilization utilization ketolysis in non-hepatic tissue such as skeletal muscle. Click to enlarge. Under conditions of low glucose availability ketogenesis occurs in the liver producing the three ketone bodies, 3-hydroxybutyrate, acetoacetate and acetone.
As summarized in Figures 2 and 3, ketolysis involves three steps, two of which are reversible reactions carried out by two 3-hydroxy butyrate dehydrogenase and acetoacetyl CoA thiolase of the four enzymes involved in ketogenesis. The first step in ketolysis is the oxidation of 3-hydroxybutyrate to acetoacetate by the reversible enzyme 3-hydroxy butyrate dehydrogenase followed by the reconstitution of acetoacetyl CoA from acetoacetate by the enzyme acetoacetyl succinyl CoA transferase also called succinyl CoA: 3-oxoacid CoA transferase SCOT.
This enzyme uses succinyl CoA, an intermediate product of the tricarboxylic acid cycle , as the CoA donor. The third and final step in ketosis is the generation of 2 molecules of acetyl CoA from CoA and acetoacetyl CoA by the reversible enzyme acetoacetyl CoA thiolase Figures 2 and 3 . Acetoacetyl succinyl CoA transferase is the rate-determining step in ketolysis .
Its activity is highest in the heart and kidney, followed by the central nervous system and skeletal muscle. Due to the sheer mass of skeletal muscle, this tissue accounts for the highest fraction of total ketone body utilization in the resting state. This phenomenon is responsible for the observed increase in circulating levels of ketone bodies during the early phases 3 days to 2 weeks of starvation, despite relatively constant rates of hepatic ketogenesis during this period .
Acetoacetyl succinyl CoA transferase activity is also present, but at very low levels, in the liver . Acetoacetyl CoA thiolase , the enzyme responsible for the final key step in ketolysis in extrahepatic tissues, tends to enhance the production of acetyl CoA from acetoacetyl CoA. Acetoacetyl CoA thiolase is also present in the liver — the primary locus of ketogenesis — where it plays a key role as the first step in ketogenesis - the creation of acetoacetyl CoA from two molecules of acetyl CoA .
Acetoacetyl CoA thiolase is a multipurpose enzyme that participates in several other metabolic pathways including fatty acid metabolism and the degradation of some amino acids . The rate of ketogenesis depends upon the activity of three enzymes. One is hormone-sensitive lipase or triglyceride lipase , which is found in peripheral adipocytes. Hormone-sensitive lipase catalyzes the conversion of triglycerides to diglycerides for further degradation to the free fatty acids lipolysis that serve as substrates for ketogenesis.
On the other hand, acetyl CoA carboxylase catalyzes the conversion of acetyl CoA to malonyl CoA, increasing the hepatic level of the primary substrate of fatty acid biosynthesis. Malonyl CoA levels vary in the liver directly according to the rate of fatty acid synthesis and inversely with the rate of fatty acid oxidation. Therefore, malonyl CoA plays a pivotal role in the regulation of ketogenesis.
Low levels of malonyl CoA stimulate transport of fatty acids into the mitochondria via the carnitine shuttle for oxidation to ketone bodies see lipolysis and lipogenesis for details. Malonyl CoA normally inhibits carnitine palmitoyltransferase 1  , the enzyme that transports fatty acyl CoA across the mitochondrial membrane. Hormone-sensitive lipase and acetyl CoA carboxylase , are exquisitely controlled by the level of circulating insulin which acts to inhibit ketogenesis , and epinephrine and glucagon which act to stimulate ketogenesis.
Metabolic Acidosis: Primary Bicarbonate Deficiency
Thus in fasting or diabetes the high levels of glucagon and low levels of insulin favor ketogenesis through the promotion of lipolysis in the adipocyte and the stimulation of fatty acid oxidation in the liver . Insulin inhibits lipolysis and ketogenesis and stimulates lipogenesis by triggering the inhibitory dephosphorylation of hormone-sensitive lipase and the activating dephosphorylation of acetyl CoA carboxylase. In the adipocytes, dephosphorylation of hormone-sensitive lipase inhibits the breakdown of triglycerides to fatty acids and glycerol, the rate-limiting step in the release of free fatty acids lipolysis from the adipocyte.
This thereby reduces the amount of substrate that is available to generate acetyl CoA via fatty acid oxidation for ketogenesis.
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