Activation of bovine and chicken liver dihydrofolate reductases and its relationship to a specific cysteine residue in their NH2-terminal amino acid sequences.

The purpose of this study was to purify and characterize the forms of cytochrome P-450 induced in chicken liver by acetone or ethanol. Using high performance liquid ion-exchange chromatography, we were able to isolate at least four different forms of cytochrome P-450 which were induced by acetone in chicken liver. All four forms of cytochrome P-450 proved to be distinct proteins, as indicated by their N-terminal amino acid sequences and their reconstituted catalytic activities. Two of these forms, also induced by glutethimide in chicken embryo liver, appeared to be cytochromes P450IIH1 and P450IIH2. Both of these cytochromes P-450 have identical catalytic activities towards benzphetamine demethylation. However, they differ in their abilities to hydroxylate p-nitrophenol and to convert acetaminophen into a metabolite that forms a covalent adduct with glutathione at the 3-position. Another form of cytochrome P-450 induced by acetone is highly active in the hydroxylation of p-nitrophenol and in the conversion of acetaminophen to a reactive metabolite, similar to reactions catalysed by mammalian cytochrome P450IIE. Yet the N-terminal amino acid sequence of this form has only 30-33% similarity with cytochrome P450IIE purified from rat, rabbit and human livers. A fourth form of cytochrome P-450 was identified whose N-terminal amino acid sequence and enzymic activities do not correspond to any mammalian cytochromes P-450 reported to be induced by acetone or ethanol.

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N-terminal amino acid sequences of the heavy and light chains of chicken liver cathepsin L

FEBS Letters ◽

10.1016/0014-5793(86)81137-1 ◽

1986 ◽

Vol 209 (2) ◽

pp. 330-334 ◽

Cited By ~ 10

Author(s):

Kenji Wada ◽

Tadashi Tanabe

Keyword(s):

Amino Acid ◽

Cathepsin L ◽

Amino Acid Sequences ◽

Chicken Liver ◽

Light Chains ◽

Terminal Amino Acid ◽

Terminal Amino

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Factor D̄ of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site

Biochemical Journal ◽

10.1042/bj1870863 ◽

1980 ◽

Vol 187 (3) ◽

pp. 863-874 ◽

Cited By ~ 34

Author(s):

D M Johnson ◽

J Gagnon ◽

K B Reid

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Alternative Pathway ◽

Amino Acid Sequences ◽

Serine Residue ◽

Amino Acid Sequence Analysis ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

The serine esterase factor D of the complement system was purified from outdated human plasma with a yield of 20% of the initial haemolytic activity found in serum. This represented an approx. 60 000-fold purification. The final product was homogeneous as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (with an apparent mol.wt. of 24 000), its migration as a single component in a variety of fractionation procedures based on size and charge, and its N-terminal amino-acid-sequence analysis. The N-terminal amino acid sequence of the first 36 residues of the intact molecule was found to be homologous with the N-terminal amino acid sequences of the catalytic chains of other serine esterases. Factor D showed an especially strong homology (greater than 60% identity) with rat ‘group-specific protease’ [Woodbury, Katunuma, Kobayashi, Titani, & Neurath (1978) Biochemistry 17, 811-819] over the first 16 amino acid residues. This similarity is of interest since it is considered that both enzymes may be synthesized in their active, rather than zymogen, forms. The three major CNBr fragments of factor D, which had apparent mol.wts. of 15 800, 6600 and 1700, were purified and then aligned by N-terminal amino acid sequence analysis and amino acid analysis. By using factor D labelled with di-[1,3-14C]isopropylphosphofluoridate it was shown that the CNBr fragment of apparent mol.wt. 6600, which is located in the C-terminal region of factor D, contained the active serine residue. The amino acid sequence around this residue was determined.

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Comparative investigations of gluten proteins from different wheat species. III. N-terminal amino acid sequences of α-gliadins potentially toxic for coeliac patients

European Food Research and Technology ◽

10.1007/s002170100365 ◽

2001 ◽

Vol 213 (3) ◽

pp. 183-186 ◽

Cited By ~ 16

Author(s):

Wieser H.

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Wheat Species ◽

Terminal Amino Acid ◽

Gluten Proteins ◽

Terminal Amino

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Comparative analyses of Serratia spp. outer membrane porin proteins

Canadian Journal of Microbiology ◽

10.1139/m93-064 ◽

1993 ◽

Vol 39 (4) ◽

pp. 442-447 ◽

Cited By ~ 1

Author(s):

Joanne Hutsul ◽

Elizabeth Worobec ◽

Tom R. Parr Jr. ◽

Gerald W. Becker

Keyword(s):

Amino Acid ◽

Serratia Marcescens ◽

Single Channel ◽

Enteric Bacteria ◽

Amino Acid Sequences ◽

Chromosomal Dna ◽

Terminal Amino Acid ◽

Molecular Weight Range ◽

Terminal Amino ◽

Porin Proteins

Eight Serratia strains and several members of the Enterobacteriaceae family were used in immunoblot and Southern DNA hybridization experiments and probed with antibody and DNA probes specific for the 41-kDa Serratia marcescens porin, to determine the extent of homology between Gram-negative porins. Immunoblot analyses performed using porin-specific rabbit sera and cell envelope preparations from these strains revealed that all strains produced at least one cross-reactive protein in the 41-kDa molecular weight range. Chromosomal DNA from each of the same strains was used in Southern analyses, probed with a 20-base-length oligonucleotide probe deduced from the N-terminal amino acid sequence of the 41-kDa Serratia marcescens porin. The probe hybridized to DNA from all of the Serratia species and six of the nine other enteric bacteria. Putative porin proteins from all the Serratia species were subjected to N-terminal amino acid sequencing and porin functional analysis using the black lipid bilayer method. All amino acid sequences were identical, with one exception in which an asparagine was substituted for an aspartic acid in Serratia rubidaea. All porins had very similar porin function (single channel conductance ranging between 1.72 and 2.00 nS). The results from this study revealed that a strong conservation exists among the Serratia porins and those produced by other enteric bacteria.Key words: porins, Serratia marcescens, homology studies.

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Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Biochemistry ◽

10.1021/bi00596a010 ◽

1978 ◽

Vol 17 (3) ◽

pp. 442-445 ◽

Cited By ~ 91

Author(s):

Mark A. Hermodson ◽

Kirk C. S. Chen ◽

Thomas M. Buchanan

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Terminal Amino Acid ◽

Amino Terminal ◽

Terminal Amino ◽

Unusual Amino Acid

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Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane

Biochemical Journal ◽

10.1042/bj2561043 ◽

1988 ◽

Vol 256 (3) ◽

pp. 1043-1046 ◽

Cited By ~ 54

Author(s):

N D Avent ◽

K Ridgwell ◽

W J Mawby ◽

M J Tanner ◽

D J Anstee ◽

...

Keyword(s):

Amino Acid ◽

Blood Group ◽

Protein Sequence ◽

Amino Acid Sequences ◽

Red Cells ◽

British Library ◽

Blood Group System ◽

Terminal Amino Acid ◽

Red Cell Membrane ◽

Terminal Amino

The Rh D blood-group antigen forms part of a complex, involving several other polypeptides, that is deficient in the red cells of individuals who lack all the antigens of the Rh blood-group system (Rhnull red cells). These include components recognized by anti-(Rh D) antibodies and the murine monoclonal antibodies R6A and BRIC 125. We have carried out protein-sequence studies on the components immunoprecipitated by these antibodies. Anti-(Rh D) antibodies immunoprecipitate an Mr-30,000-32,000 polypeptide (the D30 polypeptide) and an Mr-45,000-100,000 glycoprotein (D50 polypeptide). Antibody R6A immunoprecipitates two glycoproteins of Mr 31,000-34,000 (R6A32 polypeptide) and Mr 35,000-52,000 (R6A45 polypeptide). The D30 and R6A32 polypeptides were found to have the same N-terminal amino acid sequences, showing that they are closely related proteins. The D50 polypeptide and the R6A45 polypeptide also had indistinguishable N-terminal amino acid sequences that differed from that of the D30 and R6A32 polypeptides. The putative N-terminal membrane-spanning segments of the two groups of proteins showed homology in their amino acid sequence, which may account for the association of each of the pairs of proteins during co-precipitation by the antibodies. Supplementary data related to the protein sequence have been deposited as Supplementary Publication SUP 50417 (6 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1988) 249, 5.

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