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Showing 1 to 12 of 22 entries
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Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda.

European journal of biochemistry

Walker JE, Auffret AD, Carne A, Gurnett A, Hanisch P, Hill D, Saraste M.
PMID: 6210528
Eur J Biochem. 1982 Apr 01;123(2):253-60. doi: 10.1111/j.1432-1033.1982.tb19761.x.
Free Article

An approach to sequencing proteins by the solid-phase method combined with isolation of proteins and polypeptides by gel electrophoresis is described. Mixtures of proteins or polypeptides resulting from digests are fractionated in the presence of dodecylsulphate in polyacrylamide gels....

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Walker JE, Auffret AD, Carne A, et al. Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda. Eur J Biochem. 1982;123(2):253-60doi: 10.1111/j.1432-1033.1982.tb19761.x.
Walker, J. E., Auffret, A. D., Carne, A., Gurnett, A., Hanisch, P., Hill, D., & Saraste, M. (1982). Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda. European journal of biochemistry, 123(2), 253-60. https://doi.org/10.1111/j.1432-1033.1982.tb19761.x
Walker, J E, et al. "Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda." European journal of biochemistry vol. 123,2 (1982): 253-60. doi: https://doi.org/10.1111/j.1432-1033.1982.tb19761.x
Walker JE, Auffret AD, Carne A, Gurnett A, Hanisch P, Hill D, Saraste M. Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda. Eur J Biochem. 1982 Apr 01;123(2):253-60. doi: 10.1111/j.1432-1033.1982.tb19761.x. PMID: 6210528.
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Identification of the blocked N-terminus of an alcohol dehydrogenase from Drosophila melanogaster N-11.

FEBS letters

Auffret AD, Williams DH.
PMID: 97096
FEBS Lett. 1978 Jun 15;90(2):324-6. doi: 10.1016/0014-5793(78)80396-2.
Free Article

No abstract available.

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Auffret AD, Williams DH. Identification of the blocked N-terminus of an alcohol dehydrogenase from Drosophila melanogaster N-11. FEBS Lett. 1978;90(2):324-6doi: 10.1016/0014-5793(78)80396-2.
Auffret, A. D., & Williams, D. H. (1978). Identification of the blocked N-terminus of an alcohol dehydrogenase from Drosophila melanogaster N-11. FEBS letters, 90(2), 324-6. https://doi.org/10.1016/0014-5793(78)80396-2
Auffret, A D, and Williams, D H. "Identification of the blocked N-terminus of an alcohol dehydrogenase from Drosophila melanogaster N-11." FEBS letters vol. 90,2 (1978): 324-6. doi: https://doi.org/10.1016/0014-5793(78)80396-2
Auffret AD, Williams DH. Identification of the blocked N-terminus of an alcohol dehydrogenase from Drosophila melanogaster N-11. FEBS Lett. 1978 Jun 15;90(2):324-6. doi: 10.1016/0014-5793(78)80396-2. PMID: 97096.
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Enzyme-mediated peptide synthesis using acylpeptide hydrolase.

European journal of biochemistry

Farries TC, Auffret AD, Aitken A.
PMID: 1688346
Eur J Biochem. 1991 Mar 28;196(3):687-92. doi: 10.1111/j.1432-1033.1991.tb15866.x.
Free Article

Acylpeptide hydrolase is shown to catalyse the specific addition of a single amino acid to the N-terminus of a peptide. The stabilised Sepharose-coupled form of the enzyme is used to couple a carboxy-methylated N-formyl (or N-acetyl) amino acid to...

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Farries TC, Auffret AD, Aitken A. Enzyme-mediated peptide synthesis using acylpeptide hydrolase. Eur J Biochem. 1991;196(3):687-92doi: 10.1111/j.1432-1033.1991.tb15866.x.
Farries, T. C., Auffret, A. D., & Aitken, A. (1991). Enzyme-mediated peptide synthesis using acylpeptide hydrolase. European journal of biochemistry, 196(3), 687-92. https://doi.org/10.1111/j.1432-1033.1991.tb15866.x
Farries, T C, et al. "Enzyme-mediated peptide synthesis using acylpeptide hydrolase." European journal of biochemistry vol. 196,3 (1991): 687-92. doi: https://doi.org/10.1111/j.1432-1033.1991.tb15866.x
Farries TC, Auffret AD, Aitken A. Enzyme-mediated peptide synthesis using acylpeptide hydrolase. Eur J Biochem. 1991 Mar 28;196(3):687-92. doi: 10.1111/j.1432-1033.1991.tb15866.x. PMID: 1688346.
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Characterisation of freeze-dried wafers and solvent evaporated films as potential drug delivery systems to mucosal surfaces.

International journal of pharmaceutics

Boateng JS, Auffret AD, Matthews KH, Humphrey MJ, Stevens HN, Eccleston GM.
PMID: 20083177
Int J Pharm. 2010 Apr 15;389(1):24-31. doi: 10.1016/j.ijpharm.2010.01.008. Epub 2010 Jan 18.

Freeze-dried (lyophilised) wafers and solvent cast films from sodium alginate (ALG) and sodium carboxymethylcellulose (CMC) have been developed as potential drug delivery systems for mucosal surfaces including wounds. The wafers (ALG, CMC) and films (CMC) were prepared by freeze-drying...

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Boateng JS, Auffret AD, Matthews KH, et al. Characterisation of freeze-dried wafers and solvent evaporated films as potential drug delivery systems to mucosal surfaces. Int J Pharm. 2010;389(1):24-31doi: 10.1016/j.ijpharm.2010.01.008.
Boateng, J. S., Auffret, A. D., Matthews, K. H., Humphrey, M. J., Stevens, H. N., & Eccleston, G. M. (2010). Characterisation of freeze-dried wafers and solvent evaporated films as potential drug delivery systems to mucosal surfaces. International journal of pharmaceutics, 389(1), 24-31. https://doi.org/10.1016/j.ijpharm.2010.01.008
Boateng, Joshua S, et al. "Characterisation of freeze-dried wafers and solvent evaporated films as potential drug delivery systems to mucosal surfaces." International journal of pharmaceutics vol. 389,1 (2010): 24-31. doi: https://doi.org/10.1016/j.ijpharm.2010.01.008
Boateng JS, Auffret AD, Matthews KH, Humphrey MJ, Stevens HN, Eccleston GM. Characterisation of freeze-dried wafers and solvent evaporated films as potential drug delivery systems to mucosal surfaces. Int J Pharm. 2010 Apr 15;389(1):24-31. doi: 10.1016/j.ijpharm.2010.01.008. Epub 2010 Jan 18. PMID: 20083177.
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Comparison of the in vitro release characteristics of mucosal freeze-dried wafers and solvent-cast films containing an insoluble drug.

Drug development and industrial pharmacy

Boateng JS, Matthews KH, Auffret AD, Humphrey MJ, Eccleston GM, Stevens HN.
PMID: 21714725
Drug Dev Ind Pharm. 2012 Jan;38(1):47-54. doi: 10.3109/03639045.2011.590496. Epub 2011 Jun 30.

Drug release characteristics of freeze-dried wafers and solvent-cast films prepared from sodium carboxymethylcellulose have been investigated and compared. In vitro drug dissolution studies were performed using an exchange cell and drug release was measured by UV spectroscopy at 272...

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Boateng JS, Matthews KH, Auffret AD, et al. Comparison of the in vitro release characteristics of mucosal freeze-dried wafers and solvent-cast films containing an insoluble drug. Drug Dev Ind Pharm. 2011;38(1):47-54doi: 10.3109/03639045.2011.590496.
Boateng, J. S., Matthews, K. H., Auffret, A. D., Humphrey, M. J., Eccleston, G. M., & Stevens, H. N. (2012). Comparison of the in vitro release characteristics of mucosal freeze-dried wafers and solvent-cast films containing an insoluble drug. Drug development and industrial pharmacy, 38(1), 47-54. https://doi.org/10.3109/03639045.2011.590496
Boateng, Joshua S, et al. "Comparison of the in vitro release characteristics of mucosal freeze-dried wafers and solvent-cast films containing an insoluble drug." Drug development and industrial pharmacy vol. 38,1 (2012): 47-54. doi: https://doi.org/10.3109/03639045.2011.590496
Boateng JS, Matthews KH, Auffret AD, Humphrey MJ, Eccleston GM, Stevens HN. Comparison of the in vitro release characteristics of mucosal freeze-dried wafers and solvent-cast films containing an insoluble drug. Drug Dev Ind Pharm. 2012 Jan;38(1):47-54. doi: 10.3109/03639045.2011.590496. Epub 2011 Jun 30. PMID: 21714725.
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Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase.

Proceedings of the National Academy of Sciences of the United States of America

Howe CJ, Auffret AD, Doherty A, Bowman CM, Dyer TA, Gray JC.
PMID: 16593250
Proc Natl Acad Sci U S A. 1982 Nov;79(22):6903-7. doi: 10.1073/pnas.79.22.6903.

The proton-translocating subunit of wheat chloroplast ATP synthase is encoded by a chloroplast gene that has been accurately mapped and whose nucleotide sequence has been determined. The predicted sequence of 81 amino acids has been confirmed in part by...

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Howe CJ, Auffret AD, Doherty A, et al. Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase. Proc Natl Acad Sci U S A. 1982;79(22):6903-7doi: 10.1073/pnas.79.22.6903.
Howe, C. J., Auffret, A. D., Doherty, A., Bowman, C. M., Dyer, T. A., & Gray, J. C. (1982). Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase. Proceedings of the National Academy of Sciences of the United States of America, 79(22), 6903-7. https://doi.org/10.1073/pnas.79.22.6903
Howe, C J, et al. "Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase." Proceedings of the National Academy of Sciences of the United States of America vol. 79,22 (1982): 6903-7. doi: https://doi.org/10.1073/pnas.79.22.6903
Howe CJ, Auffret AD, Doherty A, Bowman CM, Dyer TA, Gray JC. Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase. Proc Natl Acad Sci U S A. 1982 Nov;79(22):6903-7. doi: 10.1073/pnas.79.22.6903. PMID: 16593250; PMCID: PMC347242.
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Study of 'difficult peptides' from Paracoccus cytochrome c-550 and a dolphin cytochrome c. Fast atom bombardment: a new method for molecular weight and sequence determination of peptides.

FEBS letters

Williams DH, Bojesen G, Auffret AD, Taylor LC.
PMID: 6268447
FEBS Lett. 1981 Jun 01;128(1):37-9. doi: 10.1016/0014-5793(81)81073-3.
Free Article

No abstract available.

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Williams DH, Bojesen G, Auffret AD, et al. Study of 'difficult peptides' from Paracoccus cytochrome c-550 and a dolphin cytochrome c. Fast atom bombardment: a new method for molecular weight and sequence determination of peptides. FEBS Lett. 1981;128(1):37-9doi: 10.1016/0014-5793(81)81073-3.
Williams, D. H., Bojesen, G., Auffret, A. D., & Taylor, L. C. (1981). Study of 'difficult peptides' from Paracoccus cytochrome c-550 and a dolphin cytochrome c. Fast atom bombardment: a new method for molecular weight and sequence determination of peptides. FEBS letters, 128(1), 37-9. https://doi.org/10.1016/0014-5793(81)81073-3
Williams, D H, et al. "Study of 'difficult peptides' from Paracoccus cytochrome c-550 and a dolphin cytochrome c. Fast atom bombardment: a new method for molecular weight and sequence determination of peptides." FEBS letters vol. 128,1 (1981): 37-9. doi: https://doi.org/10.1016/0014-5793(81)81073-3
Williams DH, Bojesen G, Auffret AD, Taylor LC. Study of 'difficult peptides' from Paracoccus cytochrome c-550 and a dolphin cytochrome c. Fast atom bombardment: a new method for molecular weight and sequence determination of peptides. FEBS Lett. 1981 Jun 01;128(1):37-9. doi: 10.1016/0014-5793(81)81073-3. PMID: 6268447.
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Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing.

European journal of biochemistry

Farries TC, Harris A, Auffret AD, Aitken A.
PMID: 2013290
Eur J Biochem. 1991 Mar 28;196(3):679-85. doi: 10.1111/j.1432-1033.1991.tb15865.x.
Free Article

Acylpeptide hydrolase, an enzyme that removes the modified residue from N-terminally acetylated peptides, has been purified from ovine liver and developed as a tool in sequencing blocked peptides and proteins. Its instability imposes a major limitation on the use...

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Farries TC, Harris A, Auffret AD, et al. Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing. Eur J Biochem. 1991;196(3):679-85doi: 10.1111/j.1432-1033.1991.tb15865.x.
Farries, T. C., Harris, A., Auffret, A. D., & Aitken, A. (1991). Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing. European journal of biochemistry, 196(3), 679-85. https://doi.org/10.1111/j.1432-1033.1991.tb15865.x
Farries, T C, et al. "Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing." European journal of biochemistry vol. 196,3 (1991): 679-85. doi: https://doi.org/10.1111/j.1432-1033.1991.tb15865.x
Farries TC, Harris A, Auffret AD, Aitken A. Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase. Stabilization of the enzyme and its application to protein sequencing. Eur J Biochem. 1991 Mar 28;196(3):679-85. doi: 10.1111/j.1432-1033.1991.tb15865.x. PMID: 2013290.
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Bond cleavage reactions in solid aqueous carbohydrate solutions.

Pharmaceutical research

Streefland L, Auffret AD, Franks F.
PMID: 9647348
Pharm Res. 1998 Jun;15(6):843-9. doi: 10.1023/a:1011912228954.

PURPOSE: To investigate chemical reactivity in water soluble glasses.METHODS: Rates of bond cleavage reactions in freeze-dried and freeze-concentrated aqueous carbohydrate solutions were measured above and below the glass transition temperatures (Tg). The kinetics of two reactions have been determined...

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Streefland L, Auffret AD, Franks F. Bond cleavage reactions in solid aqueous carbohydrate solutions. Pharm Res. 1998;15(6):843-9doi: 10.1023/a:1011912228954.
Streefland, L., Auffret, A. D., & Franks, F. (1998). Bond cleavage reactions in solid aqueous carbohydrate solutions. Pharmaceutical research, 15(6), 843-9. https://doi.org/10.1023/a:1011912228954
Streefland, L, et al. "Bond cleavage reactions in solid aqueous carbohydrate solutions." Pharmaceutical research vol. 15,6 (1998): 843-9. doi: https://doi.org/10.1023/a:1011912228954
Streefland L, Auffret AD, Franks F. Bond cleavage reactions in solid aqueous carbohydrate solutions. Pharm Res. 1998 Jun;15(6):843-9. doi: 10.1023/a:1011912228954. PMID: 9647348.
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In vitro drug release studies of polymeric freeze-dried wafers and solvent-cast films using paracetamol as a model soluble drug.

International journal of pharmaceutics

Boateng JS, Matthews KH, Auffret AD, Humphrey MJ, Stevens HN, Eccleston GM.
PMID: 19477255
Int J Pharm. 2009 Aug 13;378(1):66-72. doi: 10.1016/j.ijpharm.2009.05.038. Epub 2009 May 27.

Drug dissolution and release characteristics from freeze-dried wafers and solvent-cast films prepared from sodium carboxymethylcellulose (CMC) have been investigated to determine the mechanisms of drug release from the two systems. The formulations were prepared by freeze-drying (wafers) or drying...

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Boateng JS, Matthews KH, Auffret AD, et al. In vitro drug release studies of polymeric freeze-dried wafers and solvent-cast films using paracetamol as a model soluble drug. Int J Pharm. 2009;378(1):66-72doi: 10.1016/j.ijpharm.2009.05.038.
Boateng, J. S., Matthews, K. H., Auffret, A. D., Humphrey, M. J., Stevens, H. N., & Eccleston, G. M. (2009). In vitro drug release studies of polymeric freeze-dried wafers and solvent-cast films using paracetamol as a model soluble drug. International journal of pharmaceutics, 378(1), 66-72. https://doi.org/10.1016/j.ijpharm.2009.05.038
Boateng, Joshua S, et al. "In vitro drug release studies of polymeric freeze-dried wafers and solvent-cast films using paracetamol as a model soluble drug." International journal of pharmaceutics vol. 378,1 (2009): 66-72. doi: https://doi.org/10.1016/j.ijpharm.2009.05.038
Boateng JS, Matthews KH, Auffret AD, Humphrey MJ, Stevens HN, Eccleston GM. In vitro drug release studies of polymeric freeze-dried wafers and solvent-cast films using paracetamol as a model soluble drug. Int J Pharm. 2009 Aug 13;378(1):66-72. doi: 10.1016/j.ijpharm.2009.05.038. Epub 2009 May 27. PMID: 19477255.
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Structure and topology of cytochrome f in pea chloroplast membranes.

Cell

Willey DL, Auffret AD, Gray JC.
PMID: 6319031
Cell. 1984 Feb;36(2):555-62. doi: 10.1016/0092-8674(84)90248-4.

A transmembrane arrangement of cytochrome f in chloroplast thylakoid membranes, with the N-terminal heme-containing region in the intrathylakoid space and a 15 amino acid C-terminal sequence in the stroma, is suggested by the amino acid sequence deduced from the...

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Willey DL, Auffret AD, Gray JC. Structure and topology of cytochrome f in pea chloroplast membranes. Cell. 1984;36(2):555-62doi: 10.1016/0092-8674(84)90248-4.
Willey, D. L., Auffret, A. D., & Gray, J. C. (1984). Structure and topology of cytochrome f in pea chloroplast membranes. Cell, 36(2), 555-62. https://doi.org/10.1016/0092-8674(84)90248-4
Willey, D L, et al. "Structure and topology of cytochrome f in pea chloroplast membranes." Cell vol. 36,2 (1984): 555-62. doi: https://doi.org/10.1016/0092-8674(84)90248-4
Willey DL, Auffret AD, Gray JC. Structure and topology of cytochrome f in pea chloroplast membranes. Cell. 1984 Feb;36(2):555-62. doi: 10.1016/0092-8674(84)90248-4. PMID: 6319031.
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Mass spectrometric sequence studies of a superoxide dismutase from Bacillus stearothermophilus.

European journal of biochemistry

Auffret AD, Blake TJ, Williams DH.
PMID: 7202415
Eur J Biochem. 1981 Jan;113(2):333-8. doi: 10.1111/j.1432-1033.1981.tb05071.x.
Free Article

A partial sequence of the manganese-containing superoxide dismutase from Bacillus stearothermophilus has been determined by mass spectrometry. A new fragmentation reaction at N-terminal proline is described and an 'in-chain' fragmentation, also occurring at proline, has been observed. There is...

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Auffret AD, Blake TJ, Williams DH. Mass spectrometric sequence studies of a superoxide dismutase from Bacillus stearothermophilus. Eur J Biochem. 1981;113(2):333-8doi: 10.1111/j.1432-1033.1981.tb05071.x.
Auffret, A. D., Blake, T. J., & Williams, D. H. (1981). Mass spectrometric sequence studies of a superoxide dismutase from Bacillus stearothermophilus. European journal of biochemistry, 113(2), 333-8. https://doi.org/10.1111/j.1432-1033.1981.tb05071.x
Auffret, A D, et al. "Mass spectrometric sequence studies of a superoxide dismutase from Bacillus stearothermophilus." European journal of biochemistry vol. 113,2 (1981): 333-8. doi: https://doi.org/10.1111/j.1432-1033.1981.tb05071.x
Auffret AD, Blake TJ, Williams DH. Mass spectrometric sequence studies of a superoxide dismutase from Bacillus stearothermophilus. Eur J Biochem. 1981 Jan;113(2):333-8. doi: 10.1111/j.1432-1033.1981.tb05071.x. PMID: 7202415.
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Showing 1 to 12 of 22 entries