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

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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Homology of the NH2-terminal amino acid sequences of the heavy and light chains of human monoclonal lupus autoantibodies containing the dominant 16/6 idiotype.

Journal of Clinical Investigation ◽

10.1172/jci111808 ◽

1985 ◽

Vol 75 (4) ◽

pp. 1138-1143 ◽

Cited By ~ 51

Author(s):

P M Atkinson ◽

G W Lampman ◽

B C Furie ◽

Y Naparstek ◽

R S Schwartz ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Light Chains ◽

Terminal Amino Acid ◽

Terminal Amino

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The amino-terminal amino acid sequences of rabbit immunoglobulin light chains.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.55.5.1195 ◽

1966 ◽

Vol 55 (5) ◽

pp. 1195-1201 ◽

Cited By ~ 17

Author(s):

R. F. Doolittle

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Light Chains ◽

Immunoglobulin Light Chains ◽

Terminal Amino Acid ◽

Amino Terminal ◽

Rabbit Immunoglobulin ◽

Terminal Amino

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Immunoglobulin class switch from IgG to IgA in a patient with smoldering multiple myeloma

Blood ◽

10.1182/blood.v67.6.1710.1710 ◽

1986 ◽

Vol 67 (6) ◽

pp. 1710-1713 ◽

Cited By ~ 5

Author(s):

M Takahashi ◽

T Tsukada ◽

M Kojima ◽

T Koide ◽

T Koike ◽

...

Keyword(s):

Multiple Myeloma ◽

Amino Acid ◽

Amino Acid Sequences ◽

Light Chains ◽

B Cell Differentiation ◽

Terminal Amino Acid ◽

Variable Regions ◽

Class Switch ◽

Smoldering Multiple Myeloma ◽

Terminal Amino

Abstract Serum of a 67-year-old male patient with smoldering multiple myeloma was shown to contain two monoclonal immunoglobulins, IgG and IgA. For the initial seven months, monoclonal IgG was predominantly elevated. During the next one year and eight months, however, serum concentration of the monoclonal IgA increased, with a concomitant decrease of IgG. N- terminal amino acid sequences of heavy and light chains separated from monoclonal IgG and IgA were analyzed. Both light chains were lambda- type and showed identical amino acid sequences of variable regions. The heavy chains also had the same N-terminal amino acid sequence between IgG and IgA. These results strongly suggest that two monoclonal proteins, IgG and IgA, in this patient were produced by B lymphocytes within a clone and that class switch from IgG to IgA in immunoglobulin production during B cell differentiation has taken place in the clinical course of this case.

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Immunoglobulin class switch from IgG to IgA in a patient with smoldering multiple myeloma

Blood ◽

10.1182/blood.v67.6.1710.bloodjournal6761710 ◽

1986 ◽

Vol 67 (6) ◽

pp. 1710-1713

Author(s):

M Takahashi ◽

T Tsukada ◽

M Kojima ◽

T Koide ◽

T Koike ◽

...

Keyword(s):

Multiple Myeloma ◽

Amino Acid ◽

Amino Acid Sequences ◽

Light Chains ◽

B Cell Differentiation ◽

Terminal Amino Acid ◽

Variable Regions ◽

Class Switch ◽

Smoldering Multiple Myeloma ◽

Terminal Amino

Serum of a 67-year-old male patient with smoldering multiple myeloma was shown to contain two monoclonal immunoglobulins, IgG and IgA. For the initial seven months, monoclonal IgG was predominantly elevated. During the next one year and eight months, however, serum concentration of the monoclonal IgA increased, with a concomitant decrease of IgG. N- terminal amino acid sequences of heavy and light chains separated from monoclonal IgG and IgA were analyzed. Both light chains were lambda- type and showed identical amino acid sequences of variable regions. The heavy chains also had the same N-terminal amino acid sequence between IgG and IgA. These results strongly suggest that two monoclonal proteins, IgG and IgA, in this patient were produced by B lymphocytes within a clone and that class switch from IgG to IgA in immunoglobulin production during B cell differentiation has taken place in the clinical course of this case.

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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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