Echocardiographic Evaluation of Aortic Regurgitation

Sallach, Susan M.; Reimold, Sharon C.

doi:10.1007/978-1-59259-977-6_12

Cited by 12 publications

(16 citation statements)

References 32 publications

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“…Enzymes catalysing the transfer of the 8-amino group of ornithine to a number of keto acids have been described (Meister, 1953), so that taken with the 'alanine-hydroxypyruvate' transaminase catalysing serine formation (Sallach, 1956) the use of ornithine nitrogen for the mammary synthesis of all the non-essential amino acids becomes a possibility if enzyme systems which have been described in other tissues (see Greenberg, 1961) are also present in the lactating mammary gland. Verbeke, Peeters, Cocquyt & Lauryssens (1965) have reported the incorporation of [2-14C]ornithine into the proline residues of casein by a perfused sheep mammary gland.…”

Section: Discussionmentioning

confidence: 99%

A quantitative assessment of the contribution of individual plasma amino acids to the synthesis of milk proteins by the goat mammary gland

Mepham¹,

Linzell²

1966

Biochemical Journal

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1. Arteriovenous differences of plasma free amino acids across the lactating mammary glands of six goats have been measured. 2. In four experiments, measurements of blood flow, amino acid arteriovenous differences, milk yield and milk nitrogen showed that the uptake of nitrogen in the form of amino acids was sufficient to provide all the nitrogen of the milk proteins synthesized in the mammary gland. 3. In the same four experiments the uptake from the plasma and output into the milk of individual amino acids per unit time were compared. The uptakes of essential amino acids and glutamic acid were approximately equal to the corresponding output figures. The uptake of serine was consistently less than the output, and the uptake of other non-essential amino acids was very variable, in some experiments being approximately equal to the output figures and in others being considerably less. 4. As in cows, there was an uptake of ornithine in all experiments, though ornithine is absent from milk. In goats, though not in cows, the uptake of arginine was consistently greatly in excess of the requirement for arginine residues in milk protein. 5. The possible significance of the uptakes of arginine and ornithine for the synthesis of serine and other non-essential amino acids in the mammary gland is discussed. 6. The importance of clamping the external pudic vein, when sampling mammary venous blood from the caudal superficial epigastric vein, is indicated.

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Section: Discussionmentioning

confidence: 99%

A quantitative assessment of the contribution of individual plasma amino acids to the synthesis of milk proteins by the goat mammary gland

Mepham¹,

Linzell²

1966

Biochemical Journal

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“…Hydroxypyruvate is also a substrate for transketolase (Horecker, Smyrniotis & Klenow, 1953;Haba, Leder & Racker, 1955) and for carboxylases of yeast (Dickens & Williamson, 1956b) and of muscle (Dickens & Williamson, unpublished work). A transaminase present in animal tissues is able to transfer the amino group of L-alanine to hydroxypyruvate, yielding L-serine and pyruvate (Sallach, 1955(Sallach, , 1956. 3-Phosphohydroxypyruvate has also recently been synthesized (Ballou & Hesse, 1956) and its biological behaviour studied (Ichihara & Greenberg, 1957).…”

Section: The Preparation and Properties Of Lithium Hydroxypyruvatementioning

confidence: 99%

The preparation and properties of lithium hydroxypyruvate and hydroxypyruvic acid

Dickens

Williamson

1958

Biochemical Journal

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1. Coumarin when fed to rabbits is hydroxylated to 3-, 7-and 8-hydroxycoumarins, which are excreted in conjugation. This also occurs in the ferret, guinea pig, mouse and rat, the first three of which also excrete 5-hydroxycoumarin. However, not more than 25 % of the coumarin fed (dose 0 1 g./kg.) can be accounted for as conjugated glucuronic acid and ethereal sulphates excreted in the urine. 2. The ethereal sulphate and glucuronide of 3hydroxycoumarin were isolated from the urine of rabbits fed on coumarin. 7-Hydroxycoumarin was also isolated after acid hydrolysis of the urine. 5and 8-Hydroxycoumarins were not isolated but were detected in the hydrolysed urine by paper chromatography. The hydroxylation of coumarin has also been carried out with Fenton's reagent and an ascorbic acid-iron system. The results, which were not exactly the same as those found in vivo, have been discussed. 3. o-Coumaric acid appears to be excreted unchanged to a large extent by rabbits. It is, however, directly conjugated to a small extent since its ether glucuronide, o-glucosidurono-tran8-cinnamic acid, was isolated and its glycine conjugate, o-hydroxy-tran8-cinnamoylglycine, was detected by paper chromatography in the urine. 4. o-Coumaric acid % also cyclized in vivo, since small amounts of the glucuronide of 4-hydroxycoumarin were isolated from the urine and 7hydroxycoumarin was detected chromatographically. Melilotic acid, the corresponding saturated acid (dihydrocoumaric acid), also yields 4-and 7hydroxycoumarin in the rabbit. 5. The mechanism of the cyclization of o-coumaric acid has been discussed and it is suggested that the coumarin derivatives formed arise from ,-oxidation products of o-coumaric acid. The expenses of this work were defrayed by a grant from the Medical Research Council. One of us (J.A.R.M.) is grateful to the Council for a maintenance grant.

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“…The penultimate step is catalysed by a specialized phosphoserine:-ketoglutarate aminotransferase (EC 2.6.1.52). A nonphosphorylated serinedegradation pathway also exists in animals (Walsh & Sallach, 1966) and plants (Liepman & Olsen, 2001) in which the amino group is added or removed by serine:pyruvate aminotransferase (EC 2.6.1.51; SPAT) or serine:glyoxylate aminotransferase (EC 2.6.1.45) (Sallach, 1956). Serine aminotransferases are also found in some bacteria (Izumi et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase fromSulfolobus solfataricus

Sayer

Bommer

Isupov

et al. 2012

Acta Crystallogr D Biol Cryst

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The three‐dimensional structure of the Sulfolobus solfataricus serine:pyruvate aminotransferase has been determined to 1.8 Å resolution. The structure of the protein is a homodimer that adopts the type I fold of pyridoxal 5′‐phosphate (PLP)‐dependent aminotransferases. The structure revealed the PLP cofactor covalently bound in the active site to the active‐site lysine in the internal aldimine form. The structure of the S. solfataricus enzyme was also determined with an amino form of the cofactor pyridoxamine 5′‐phosphate bound in the active site and in complex with gabaculine, an aminotransferase inhibitor. These structures showed the changes in the enzyme active site during the course of the catalytic reaction. A comparison of the structure of the S. solfataricus enzyme with that of the closely related alanine:glyoxylate aminotransferase has identified structural features that are proposed to be responsible for the differences in substrate specificity between the two enzymes. These results have been complemented by biochemical studies of the substrate specificity and thermostability of the S. solfataricus enzyme.

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Echocardiographic Evaluation of Aortic Regurgitation

Cited by 12 publications

References 32 publications

A quantitative assessment of the contribution of individual plasma amino acids to the synthesis of milk proteins by the goat mammary gland

A quantitative assessment of the contribution of individual plasma amino acids to the synthesis of milk proteins by the goat mammary gland

The preparation and properties of lithium hydroxypyruvate and hydroxypyruvic acid

Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase fromSulfolobus solfataricus

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