Formation of ∈-(aminosuccinyl)-lysine from ∈-aspartyl-lysine from bacitracin A, and from the cell walls of lactobacilli

Swallow, D. L.; Abraham, E. P.

doi:10.1042/bj0700364

Cited by 86 publications

(33 citation statements)

References 19 publications

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“…Densitometric trace of gel scanned at 350 nm. (Swallow & Abraham, 1958;Naughton, Sanger, Hartley & Shaw, 1960). Components I and IV have not yet been identified.…”

Section: Bioassaysmentioning

confidence: 94%

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Storring¹,

Gaines-Das²,

Tiplady³

et al. 1980

Journal of Endocrinology

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The corticotrophin activity of ampoules of the Third International Standard for Corticotrophin (IS) kept at 20 and 37 \ s=deg\ Cfor 15 years was compared with that of ampoules of the IS stored under normal conditions ( \ m=-\ 20 \s=deg\Cin the dark), using adrenal ascorbate depletion assays after subcutaneous administration of the hormone, assays of an increase in plasma corticosterone after intravenous administration of the hormone and in-vitro adrenal cell corticosterone production assays. Estimates of activity by all three methods are homogeneous and give combined weighted geometric means (with 95% confidence limits), as per cent of the activity in the IS stored at \m=-\20 \ s=deg\ C, of 92\m=.\1(84\m=.\8\p=n-\100) and 77\m=.\8(71\ m=. \ 6\ p=n-\ 84\ m=. \ 5) for the 20 and 37 \ s=deg\ C degradation samples respectively. Isoelectric focusing studies of the ampoule contents of the three preparations showed that ampoules of the IS stored at 20 and 37 \ s=deg\ Ccontained 90 and 79% respectively, of the component representing native corticotrophin found in the IS. These estimates of corticotrophin content are comparable to the estimates of biological activity of these preparations.The stability of the IS was calculated from the combined bioassay data assuming that degradation follows first order kinetics. The predicted half-life for the activity of the IS is 2800 years with an approximate lower 95% confidence limit of 500 years; the predicted activity of the IS remaining now, after 20 years at \m=-\20\ s=deg\ C, is 99\m=.\5% of the original activity with an approximate lower 95% confidence limit of 97\m=.\3%

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“…Densitometric trace of gel scanned at 350 nm. (Swallow & Abraham, 1958;Naughton, Sanger, Hartley & Shaw, 1960). Components I and IV have not yet been identified.…”

Section: Bioassaysmentioning

confidence: 94%

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Storring¹,

Gaines-Das²,

Tiplady³

et al. 1980

Journal of Endocrinology

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“…Some a-and 8-aspartyl peptides interconvert under acid conditions, and the p structure is more stable (John and Young, 1954;Swallow and Abraham, 1958;Bryant et al, 1959). Unpublished data show that some interconversion occurs with the aspartylglycines even in water a t 37".…”

Section: Sismentioning

confidence: 99%

“…The most abundant of these, p-aspartylglycine, was shown not to arise by isomerization of a-aspartylglycine (John and Young, 1954;Swallow and Abraham, 1958; Byrant et al, 1959) during the isolation procedure, and it is likely that the other @-aspartyl oligopeptides found are actually excreted in the fl form. The present paper reports *Supported in part by Grant A-1277 from the United States Public Health Service.…”

mentioning

confidence: 99%

Studies on the in vivo Metabolism of α- and β-Aspartylglycine-1-C^14*

Buchanan¹,

Haley²,

Markiw³

et al. 1962

Biochemistry

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Human subjects were given 4-mg intravenous doses of a-~-aspartylglycine-l-C~~, P-Laspartylglycine-1-C 4, or an equivalent molar amount of free g1y~ine-l-C'~ and unlabeled aspartic acid. Much more radioactivity appeared in the expired carbon dioxide, in the urinary hippuric acid, and in the glycine and serine of plasma protein when the a rather than the p peptide was given. The results with free glycine and the a peptide were similar. When the p peptide was administered most of the radioactivity promptly appeared in the urine in the same chemical form but mixed with a larger quantity of endogenous p-aspartylglycine.The accompanying report from this laboratory (Buchanan et d., 1962) describes the isolation and identification of a number of B-aspartyl and yglutamyl oligopeptides from human urine. The most abundant of these, p-aspartylglycine, was shown not to arise by isomerization of a-aspartylglycine (John and Young, 1954;Swallow and Abraham, 1958; Byrant et al., 1959) during the isolation procedure, and it is likely that the other @-aspartyl oligopeptides found are actually excreted in the fl form. The present paper reports *Supported in part by Grant A-1277 from the United States Public Health Service. Preliminary reports (Haley et al., 1961; Buchanan at al., 1961) have appeared. studies on the metabolic fates of synthetic aand 8-aspartylglycines given intravenously to human subjects. The results support a hypothesis (Buchanan et aZ., 1962) that may explain the presence of P-aspartyl peptides in urine. METHODSThe wand P-L-aspartylglycines were prepared from carbobenzoxy-L-aspartic acid and glycine-l-C14 by a slight modification of the procedure of LeQuesne and Young (1952), separated chromatographically, and recrystallized from alcohol !Buchanan et d., 1962). The specific radioactivity of crystalline peptides was 2.5 pc per mg.

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“…Another possible explanation [12]. [12] with aspartyl peptides from the active sites of proteolytic enzymes by N a u g h to n et al [13], and with a-and //-L-aspartyl-L-valine by J o h n and Y o u n g [14]. Howev er, the conditions required to bring about the «-//-rearrangement are re latively vigorous, e.g.…”

Section: Analysis Of the Abnormal Haemoglobinmentioning

confidence: 99%

“…The simplest explanation would be that the peptide bond between Ala 129 and Asp 130 is excep tionally labile and was hydrolysed during the elution with 0.5% formic acid, although this seems rather unlikely. Another possible explanation [12]. [12] with aspartyl peptides from the active sites of proteolytic enzymes by N a u g h to n et al [13], and with a-and //-L-aspartyl-L-valine by J o h n and Y o u n g [14].…”

Section: Analysis Of the Abnormal Haemoglobinmentioning

confidence: 99%

Structure of Haemoglobin Wien <i>β</i>130 (H8) Tyrosine-Aspartic Acid; an Unstable Haemoglobin Variant

Lorkin¹,

Pietschmann²,

Braunsteiner³

et al. 1974

Acta Haematol

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Formation of ∈-(aminosuccinyl)-lysine from ∈-aspartyl-lysine from bacitracin A, and from the cell walls of lactobacilli

Cited by 86 publications

References 19 publications

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Studies on the in vivo Metabolism of α- and β-Aspartylglycine-1-C^14*

Structure of Haemoglobin Wien <i>β</i>130 (H8) Tyrosine-Aspartic Acid; an Unstable Haemoglobin Variant

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Formation of ∈-(aminosuccinyl)-lysine from ∈-aspartyl-lysine from bacitracin A, and from the cell walls of lactobacilli

Cited by 86 publications

References 19 publications

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Stability of the Third International Standard for Corticotrophin: Accelerated Degradation Study Using Different Bioassays and Isoelectric Focusing

Studies on the in vivo Metabolism of α- and β-Aspartylglycine-1-C14*

Structure of Haemoglobin Wien <i>β</i>130 (H8) Tyrosine-Aspartic Acid; an Unstable Haemoglobin Variant

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Product

Resources

About

Studies on the in vivo Metabolism of α- and β-Aspartylglycine-1-C^14*