Akira Tsugita

NEC (Japan)

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Masaharu Kamo

Iwate Medical University

Kazuo Satake

Fukui CardioVascular Center

Masayori Inouye

Rutgers, The State University of New Jersey

Lu‐Ping Chow

Vision Australia

Norifumi Miyatake

Tokyo University of Science

Peter Schürmann

Medizinische Hochschule Hannover

Keiji Takamoto

Albert Einstein College of Medicine

George Streisinger

University of Oregon

Kenji Miyazaki

Tsukuba Medical Center Hospital

Takao Kawakami

Shinshu University

Cooperative Institutions

Osaka University

The University of Tokyo

Tokyo University of Science

National Institutes of Health

Centre National de la Recherche Scientifique

Kyoto University

University of Basel

Harvard University

University of Washington

Japan Science and Technology Agency

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Escherichia coli K12 genomic database.

PubMed (1990)

T Kunisawa Masayuki Nakamura Hidemi Watanabe Jun Otsuka Akira Tsugita

We have compiled the genomic nucleic acid sequence data of Escherichia coli K12 available from the existing major data collections and from the literature. The collected data are structured as a database for easy access and analysis. The sequence segments in the database are ordered by genetic map position. Sequence redundancy has been completely removed by combining overlapping sequences; therefore, our sequence data are amenable to statistical analysis. We have specified with a plus or minus (+ or -) on which of the two DNA strands the segment exists. The database currently contains a total of 954,392 bp, which corresponds to about 20% of the entire genome size. The sequence data are available on request.

Sequence (biology)

genomic DNA

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Citations (17)

Primary structure of internal peptide VII of T-even bacteriophages

Journal of Molecular Biology (1977)

Jean Paul van Eerd Sewell P. Champe L. Yager I. Kubota Akira Tsugita

Sephadex

Protein primary structure

Cleavage (geology)

10.1016/0022-2836(77)90141-3

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Citations (9)

The Amino Acid Sequence of T4 Phage Lysozyme

Journal of Biological Chemistry (1971)

Masayori Inouye Marcelo Jacobs‐Lorena Akira Tsugita

Abstract The correct figures for Fig. 1 (p. 3468) and Fig. 2 (p. 3477) are given below : FIG. 1. Elution profile of the peptic peptides of unoxidized T4 at phage lysosyme (80 mg) on a Dowex 50-×2 column (0.9 × 150 cm). Elution was carried out with a gradient of pyridine-acetate buffer established by means of a nine-chamber Varigrad apparatus (1). The profile was obtained by measuring the absorbance 570 mμ after alkaline hydrolysis of aliquots of alternate tubes followed by ninhydrin reaction. The peptides recovered from each peak are indicated in the figure. The arrow indicate the position where P92-102 was eluted during peptidel separation of a performic acid-oxidized digest. We suggest that subscribers photocopy these corrections and insert the photocopies at the appropriate places where the article to be correctcd originally appeared. Authors are urged to introduce these corrections into any reprints they distribute. Secondary (abstract) services are urged to carry notice of these corrections as prominently as they carried the original abstracts.

Sequence (biology)

10.1016/s0021-9258(18)62146-5

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Citations (15)

Developmental Proteome Analysis of Caenorhabditis elegans

Journal of the Mass Spectrometry Society of Japan (2003)

Takuji Nabetani Yo Tabuse Akira Tsugita

Animal development proceeds through harmonized expression of many genes. A small free-living soil nematode, Caenorhabditis elegans, has many advantages as a model organism and has been used to study the genetic program, operating in animal development. In recent years, exhaustive measurement of mRNA level using DNA microarray have been carried out in various biological systems, including C. elegans and have provided valuable information about gene expression during development. On the other hand, it is often pointed out that analyses of protein level might be rather critical, since the function of a gene is accomplished by the expressed protein. To identify proteins which are expressed differentially during development and to delineate the correlation of mRNA and protein expression in C. elegans, we have conducted differential two-dimensional electrophoresis of protein samples from the embryo to adult animal. Differential image analysis of gel patterns revealed that many proteins were expressed stage-specifically and they were analyzed with MALDI-TOF mass-spectrometry. In this report, we show the result of ten proteins which expressed mainly either in the embryo or in other developmental stages besides the embryo. Although expression patterns of most of them were found to be correlated with those of mRNA level, the expression pattern of DIM-1 protein is inconsistent with that of mRNA. The discrepancy between protein and mRNA levels found in our limited scale of experiment further strengthen the notion that gene expression does not always parallel with the expression of the corresponding protein.

Proteome

Model Organism

Developmental Biology

10.5702/massspec.51.499

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Citations (1)

A Programmable Fragmentation Analysis of Proteins by In-Source Decay in MALDI-TOF Mass Spectrometry

Analytical Chemistry (2002)

Jialing Gao Akira Tsugita Mitsuo Takayama Lin Xu

Here we describe an algorithm for identifying peptides/proteins of known sequence and unknown peptides from partial spectra generated by an in-source decay (ISD) technique coupled with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The identification of protein fragments is processed with a software program called CMATCH, which generates candidate subsequences for both known peptides/proteins and unknown peptides for the major product ions in the spectral range m/z 400−5000 and then matches these to known protein sequences contained in a reference database for the known peptides/proteins. CMATCH, which is compiled for MSDOS or WINDOWS95/NT, has two main advantages: first, the candidate subsequences are generated automatically without the need for supplementary information concerning the distribution of either N-terminal or C-terminal ions in the spectra for both known peptides/proteins and unknown peptides; second, the highest coordinated homologous sequences are picked up automatically from the reference database as the best matches with known peptides/proteins. Examples from the ISD spectra of several test proteins demonstrate the efficacy of this protein identification software.

Fragmentation

10.1021/ac010900d

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Citations (14)

Amino acid sequence of ferredoxin isolated from Cyanidium caldarium strain RK-1.

PubMed (1989)

Hideyuki Nagashima Kiyofumi Sakai Masaharu Kamo Akira Tsugita

Ferredoxin was isolated from ther eukaryotic alga Cyanidium caldarium strain RK-1 and its amino acid sequence was determined. The ferredoxin is composed of 97 amino acid residues, and its molecular weight is 10,599 excluding the iron-sulfur cluster. The amino acid sequence differs from that of C. caldarium strain 1355/1, by 24 amino acid substitutions plus one deletion at the amino terminus.

Strain (injury)

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Citations (8)

Sequence information of peptides and proteins with in-source decay in matrix assisted laser desorption/ionization-time of flight-mass spectrometry

Electrophoresis (2000)

Mitsuo Takayama Akira Tsugita

In-source decay coupled with matrix assisted laser desorption/ionization-mass spectrometry, which is a mass spectrometric degradation method for the sequencing of peptides and proteins, has been applied to several different polypeptides and proteins. The influence of the nature of the constituent amino acids on positively charged product ions is described. Relatively small molecular mass peptides produced c-, b-, and/or a-series ions usable for C-terminal sequencing as well as y- and/or z-series ions usable for N-terminal sequencing. The formation of the C-terminal sequencing ions (c, b and a) and the N-terminal sequencing ions (y and z) was strongly dependent on the location(s) of basic arginine and lysine residues. The presence of the arginine and/or lysine residues at the N-terminal region was one-sided in the formation of c-, b-, and/or a-series ions, while the presence of those at the C-terminal region was favorable for the formation of y- and z-series ions. In-source decay experiments of intact proteins, apomyoglobin and two viral coat proteins, led to large amounts of c-series ions and small amounts of y-series ions, which reflected internal sequences.

Fast atom bombardment

10.1002/(sici)1522-2683(20000501)21:9<1670::aid-elps1670>3.3.co;2-e

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Citations (4)

The purification of an acid‐ and heat‐labile transforming growth factor from an avian sarcoma virus‐ transformed rat cell line

Journal of Cellular Physiology (1984)

Kazuko Yamaoka Reiko Hirai Akira Tsugita Hiromi Mitsui

A new class of transforming growth factor (TGF), with chemical characteristics differing from previously reported TGFs, was isolated and purified from an avian sarcoma virus-transformed rat cell line, 77N1 . Purification steps were simple and consisted of ion-exchange chromatography on diethylaminoethyl (DEAE)-Sephacel, ammonium sulfate precipitation, Chromatofocusing, and DEAE-Sephadex A-25 chromatography. The purified TGF is a heat- and acid-labile protein with a molecular mass of 12,000 daltons and isoelectric point of 5.2-5.4. Because of the acid lability of this TGF, purification was carried out at neutral pH. The TGF induced DNA synthesis in growth-arrested BALB 3T3 cells and promoted anchorage-independent growth of nontransformed BALB 3T3 cells in soft agar; the latter activity is specific for the peptide growth factors, called TGFs, but it did not compete with epidermal growth factor (EGF) for binding to the EGF membrane receptors. The TGF activity was not potentiated by EGF. The purified preparation of the TGF stimulated BALB 3T3 cells to grow progressively in soft agar at a dose of 20 ng/ml.

Ammonium sulfate precipitation

Chromatofocusing

3T3 cells

Molecular mass

Ion chromatography

Sephadex

10.1002/jcp.1041190308

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Citations (18)

Chromatogaphy of Crystalline Taka-Amylase a on a Weak Anion Exchanger

The Journal of Biochemistry (1959)

Akira Tsugita Masayori Inoue Shiro Akabori

Journal Article Chromatogaphy of Crystalline Taka-Amylase a on a Weak Anion Exchanger Get access Akira Tsugita, Akira Tsugita From theLaboratory of Biochemistry, Faculty of Science, Osaka University,Osaka Search for other works by this author on: Oxford Academic PubMed Google Scholar Masayori Inoue, Masayori Inoue From theLaboratory of Biochemistry, Faculty of Science, Osaka University,Osaka Search for other works by this author on: Oxford Academic PubMed Google Scholar Shiro Akabori Shiro Akabori From theLaboratory of Biochemistry, Faculty of Science, Osaka University,Osaka Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 46, Issue 1, January 1959, Pages 93–95, https://doi.org/10.1093/jb/46.1.93 Published: 01 January 1959 Article history Received: 30 August 1950 Published: 01 January 1959

Anion exchanger

10.1093/jb/46.1.93

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Citations (0)

Change of a sequence of amino acids in phage T4 lysozyme by acridine-induced mutations.

Proceedings of the National Academy of Sciences (1966)

Eric Terzaghi Yasushi Okada George Streisinger Joyce Emrich Masayori Inouye

Acridine

Sequence (biology)

Muramidase

10.1073/pnas.56.2.500

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Citations (95)