Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

Offord, Robin E.

doi:10.1038/211591a0

Cited by 1,004 publications

(475 citation statements)

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“…on an aluminium sheet of silica gel F254 (E. Merck Co.) (Niederweiser, 1972 Determination of amides of aspartic acid and glutamic acid. Amides were assigned on the basis of electrophoretic mobility of the parent peptides at pH 6.5 by the method of Offord (1966) or by chromatographic determination of glutamine and asparagine in the digests of peptides with leucine aminopeptidase or carboxypeptidase A on an amino acid analyser.…”

Section: Methodsmentioning

confidence: 99%

The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

Sato

Uchida

1975

Biochemical Journal

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1. RNAase (ribonuclease) U2, a purine-specific RNAase, was reduced, aminoethylated and hydrolysed with trypsin, chymotrypsin and thermolysin. On the basis of the analyses of the resulting peptides, the complete amino acid sequence of RNAase U2 was determined. 2. When the sequence was compared with the amino acid sequence of RNAase T1 (EC 3.1.4.8), the following regions were found to be similar in the two enzymes;

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Section: Methodsmentioning

confidence: 99%

The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

Sato

Uchida

1975

Biochemical Journal

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“…For the peptides the amino acid composition (tool per tool of peptide) and the electrophoretic behaviour and charge at pH 6.5 as determined by the method of Offord [9] are given.…”

Section: Table I Amino Acid Composition (Mol Per Mol Of Protein) Of Pmentioning

confidence: 99%

“…Peptides were separated on Sephadex G50 and G25 (Pharmacia, Uppsala, Sweden), by high voltage electrophoresis and by paper chromatography as described before [8]. The charges of peptides were estimated from their electrophoretic mobility at pH 6.5 [9]. Small peptides were sequenced according to a manual Edman procedure [ 10] in combination with dansylation [ 11].…”

mentioning

confidence: 99%

The amino acid sequence of the phospholipase A2 isoenzyme from porcine pancreas

Puijk¹,

Verheij²,

Wietzes³

et al. 1979

Biochimica et Biophysica Acta (BBA) - Protein Structure

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SummaryThe primary structure of porcine pancreatic isophospholipase A2 (EC 3.1.1.4) has been investigated. The sequence of porcine isophospholipase differs from the sequence of porcine phospholipase by four substitutions; viz. Ala 12 ~Thr; His 17 ÷Asp; Met 2° ~Leu and Glu 71 *Asn.Phospholipase A2 (EC 3.1.1.4) has been isolated from several sources, including mammalian pancreas, snake and bee venom [1,2]. The primary structures of all vertebrate phospholipases have been shown to be homologous [ 2,3 ] although the differences between individual phospholipases can be as big as fifty percent.Both snake venoms and mammalian pancreas were found to contain isoenzymes [2]. Usually the enzymes and isoenzymes which can be isolated from one animal species are characterized by relatively few substitutions. Studies concerning structure-function relationships which make use of enzymes from one animal species would be more straightforward than a comparison of phospholipases from e.g. porcine and equine pancreas.From porcine pancreas about 5% of the phospholipase can be isolated as an isoenzyme; both enzymes are very similar with respect to binding of Ca 2÷, monomeric and micellar substrate, but the isoenzyme shows a lower activity when assayed in the egg-yolk assay [4,5]. Amino acid analyses showed that the isoenzyme contains one histidine and one methionine residue less than the major occuring enzyme and evidence was obtained that His 17 and Met 2° are lacking from the sequence [4].The isoenzyme has been used for chemical modification of the single

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“…The earliest attempt is attributed to Offord [111], who has shown a linear relationship between paper electrophoretic mobilities of a series of charged peptides and their molecular mass to the power of À2/3. In principle according to Equation (1)…”

Section: Determination Of Absolute Mobility and Of Its Relation To Chmentioning

confidence: 99%

Capillary electrophoretic analysis of proteins and peptides of biomedical and pharmacological interest

Righetti

2001

Biopharm & Drug Disp

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Capillary electrophoresis (CE) is an automated approach to electrokinetic separations that has had a deep impact in all fields of life sciences, including biomedical and biotechnological research and clinical and forensic practice. The present review highlights aspects of peptides and proteins separations, with particular emphasis on macromolecular analytes of biomedical interest. Among the various CE techniques available, a novel methodology is here illustrated consisting in separations in acidic, isoelectric buffers, which have the advantage of protonating the silica wall, thus minimizing interactions of proteinaceous material with the siliceous surface, while allowing delivery of high voltage gradients, due to their low conductivities. The review ends with applications of CE to the analysis of folding/unfolding/refolding/misfolding of proteins, a field which has deep implications in the biomedical arena, since it is connected to a host of disorders, such as prion protein diseases.

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Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

Cited by 1,004 publications

References 4 publications

The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

The amino acid sequence of the phospholipase A2 isoenzyme from porcine pancreas

Capillary electrophoretic analysis of proteins and peptides of biomedical and pharmacological interest

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