Polyquarternary amines prevent peptide loss from sequenators

Tarr, George E.; Beecher, James F.; Bell, Michael V.; McKean, David J.

doi:10.1016/0003-2697(78)90086-6

Cited by 444 publications

(123 citation statements)

References 14 publications

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“…Furthermore, use of the inert carrier polybrene (29) greatly facilitated the sequence analysis of small peptides and in the case of SP-7 and SP-8 allowed the complete amino acid sequence to be determined. However, peptide SP-7, obtained from reduced and Scarboxymethylated SOD, either with or without polybrene could not be fully sequenced.…”

Section: Discussionmentioning

confidence: 99%

“…However, reagent R2 was 0.1 M-THEED replacing 1.0 M-Quadrol and the $2 wash was ethyl acetate, 15 % in propanol and 0.1% in acetic acid (3). The Beckman program 122974 (single cleavage, fast protein Quadrol) was used throughout the analyses but with the time for the $2 wash reduced from 600 to 400 seconds in step 29.…”

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

“…In the case of peptides, smaller than 30 residues, 100 01 of polybrene (30 mg.ml -I in H20) was added to the sample as suggested by TARR et al (29). In contrast to TARR et al, we have not experienced any problem with polybrene in our identification of the PTHderivative in Step 1 and hence we have omitted the dummy step as recommended by these authors.…”

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

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The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

Johansen

Overballe-Petersen

Martin

et al. 1979

Carlsberg Res. Commun.

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The amino acid sequence of the copper,zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55 96 identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the ye,~st enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor. Superoxide dismutases (SOD) are a group of metalloenzymes, whose function is to scavenge the superoxide radical anion 02 (12) by catalyzing its dismutation to hydrogen peroxide and dioxygen:

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Section: Discussionmentioning

confidence: 99%

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

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The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

Johansen

Overballe-Petersen

Martin

et al. 1979

Carlsberg Res. Commun.

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“…The amino acid sequence of the peptide was analysed with a JEOL 47KS Sequence Analyzer using polybrene [8] and a program recommended by the manufacturer with slight modifications. Thiazolinones collected were converted to phenythiohydantoins (PTH-amino acids) as in [9].…”

Section: Sequence Analysismentioning

confidence: 99%

Amino acid sequence around the active site cysteine residue of calcium‐activated neutral protease (CANP)

Suzuki

Hayashi

et al. 1983

FEBS Letters

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The active site of calcium-activated neutral protease (CANP) was specifically labeled with iodoacetic acid. The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined. The sequence indicates that CANP is a thiol protease and its comparison with other thiol proteases is described. Cal+-Activated neutral protease Active siteThiol protease Amino acid sequence Carboxymethylation

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“…The original idea was to provide a means for degrading insolubilized peptides and thus prevent the well-known 'washout' problem common to the liquid-phase instruments. Alternatively various groups have attempted to render the peptide or protein more polar (thus reducing its solubility in organic solvents) but only through the recent use of polybrene [6,7] has liquid-phase sequencing for most peptides at low concentrations (<50 nmol) become possible. In solid-phase technology on the other hand, emphasis has been directed toward improving coupling yields and providing the means to couple peptides arising from a variety of specific cleavages.…”

Section: Introductionmentioning

confidence: 99%