Biochemistry of Fishes

Tarr, H. L. A.

doi:10.1146/annurev.bi.27.070158.001255

Cited by 114 publications

(13 citation statements)

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“…By comparison with the hexose phosphates, ribose I-phosphate should be inert and ribose 5-phosphate should be somewhat more reactive per mole than free ribose, which does contribute much Maillard-reactive carbonyl to spoiling muscle.249 25a9 30 The pattern of rise and fall in the concentrations of ribose 5-phosphate found in chill-stored codling was strikingly similar to that of free ribose.lg An earlier discussion of the contribution of free ribose to the ' browning ' potential of dehydrated spoiling codling,2zb would also apply to the 5-phosphate. By comparison with the hexose phosphates, ribose I-phosphate should be inert and ribose 5-phosphate should be somewhat more reactive per mole than free ribose, which does contribute much Maillard-reactive carbonyl to spoiling muscle.249 25a9 30 The pattern of rise and fall in the concentrations of ribose 5-phosphate found in chill-stored codling was strikingly similar to that of free ribose.lg An earlier discussion of the contribution of free ribose to the ' browning ' potential of dehydrated spoiling codling,2zb would also apply to the 5-phosphate.…”

Section: Analytical Proceduresmentioning

confidence: 99%

Changes in sugar phosphates of chilled codling (Gadus callarias) muscle

Burt¹,

Jones²

1961

J Sci Food Agric

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Hexose and pentose phosphates in extracts of codling muscle havz been identified and estimated by quantitative ion-exchange chromatography. Changes in glucose I-and 6-phosphate, fructose I-and 6-phosph$te, fructose T ,6-diphosphate, ribose I-and ribose 5-phosphate and an unidentified pentose phosphate were followed throughout a period of chill storage. The findings arc discussed in relation t o their significance in comparative biochemistry and fish technology. Glucose G-ph?,sphate and fructose 1,6-diphospliate were present in concentrations a t which they would contribute significantly to the ' browning ' of muscle dehydrated fresh : ribose j-phcsphate would probably contribute to that of codling dehydrated in a spoiling condition.

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Section: Analytical Proceduresmentioning

confidence: 99%

Changes in sugar phosphates of chilled codling (Gadus callarias) muscle

Burt¹,

Jones²

1961

J Sci Food Agric

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“…R. A. McLeod [personal communication cited by Tarr (1958)] has determined QO values for tissue slices from adult coho salmon and found the following decreasing order of activity: brain, heart, liver, kidney, red lateral muscle and ordinary skeletal muscle. The low uptake and storage capacity of the white muscle of fish for oxygen is not surprising in view of the low concentrations of myohaemoglobin in that tissue.…”

Section: Resultsmentioning

confidence: 99%

Quinones and related compounds in fish tissues

Pennock¹,

Morton²,

Lawson³

et al. 1962

Biochemical Journal

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“…The phenylthiohydantoin (PTH) derivatives of the amino acids were determined quantitatively by an adaptation of the procedure described by Tari- (28), using a reverse phase column (0.62 x 15 cm) of octadecylsilane-coated 3 p m silica (ODs TI, Custoni LC, CEL Associates, Houston, TX 77072).…”

Section: Materials a N D Methodsmentioning

confidence: 99%

Characterization of cleavage products in selected human lutropin preparations

Ward

Glenn

Nahm

et al. 1986

International Journal of Peptide and Protein Research

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Low molecular weight fragments derived from the beta subunit of human lutropin have been frequently observed. These fragments are detected by polyacrylamide gel electrophoresis in sodium dodecyl sulfate following reduction of the disulfide bonds. A sample of human lutropin was identified that had a major portion of its beta subunit showing this proteolytic nick. Over 83% of the subunit was nicked based on reduction, carboxymethylation, and isolation of the low molecular weight fragments. This preparation had 53% of the activity of an intact human lutropin (radioligand assay). The proteolytic nick in the subunit was shown by N‐terminal sequencing of the C‐terminal fragments to be derived from three clips in a hexapeptide region (residues 44–49) characterized by hydrophobic alkyl side chains. Specific clips were on the amino side of Leu‐45 (8%), Val‐48 (45%) and Leu‐49 (47%). Thus the proteolytic activity, presumably derived from the pituitary during processing, has a substrate specificity reminiscent of the bacterial protease, thermolysin.

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Biochemistry of Fishes

Cited by 114 publications

References 0 publications

Changes in sugar phosphates of chilled codling (Gadus callarias) muscle

Changes in sugar phosphates of chilled codling (Gadus callarias) muscle

Quinones and related compounds in fish tissues

Characterization of cleavage products in selected human lutropin preparations

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