はまだ みのる   

濱田 稔     男

1934 11 20

 
E-MAIL: enzymes@bronze.ocn.ne.jp (勤務先)
mhamada@med.miyazaki-u.ac.jp

1953.3 佐賀県立唐津高等学校普通科卒業
1954.4 佐賀大学文理学部化学専攻入学
(1955. 2 中途退学、病気の為、自宅療養)
1956.4 長崎大学医学部進学過程入学(1958. 4 専門課程入学)
1962.3 長崎大学医学部医学科卒業
1962.4 九州大学医学部付属病院にて実地修練(1963. 3 修了)
1963.4 長崎大学大学院医学研究科博士課程、
病理系病態生化学専攻入学、67年単位取得退学
1969.11 長崎大学大学院医学研究科博士課程の修了



1963.4 第34回医師国家試験合格
(1963. 5 医師免許証下附、医籍登録第182340号)

1967.4 文部教官長崎大学助手
(医学部付設原爆後障害医療研究施設異常代謝部門)
1970.10 文部教官長崎大学講師(医学部 同上)
1971.10 文部教官長崎大学助教授(医学部 同上)
1974.9 第3回国際アイソザイム会議シンポジウム(エール大学に招待される。研究打ち合わせのため大学、研究所訪問、1ヶ月)
1975.1 特別研究員、米国ユタ大学医学部生化学・遺伝性代謝病研究所
(Dr. S.A. Kuby)に遺伝性筋肉疾患の研究のために留学
1977.1 同上、滞在延長のため、休職
1977.10 同上、終了。文部教官長崎大学助教授(医学部、同上)復職
1978.3 文部教官愛媛大学助教授(医学部、衛生学)配置換
1979.5 訪問教授米国ユタ大学医学部生化学に文部省在外研究員(甲、短期)派遣にて研究に従事(3ヶ月)
1981.7 訪問教授米国ユタ大学医学部生化学遺伝性代謝病研究所にて、
遺伝性筋肉疾患の研究に従事(2ヶ月)
1982.4 第66回米国実験生物学会(FASEB)(ニューオーリンズ)に発表のため出席、
他大学研究所訪問(1ヶ月)
1984.10 文部教官宮崎医科大学教授(医学部、衛生学)現在に至る。
1985.9 米国NIEHS(Dept. Pharmacy, Virginia)およびNIH(Genetic Lab., Triangle Park,
NIH眼病理研究所(Bethesda)においてセミナーに招待される。
1986.5 第5回国際アイソザイム会議(ギリシャ、Cos)に招待される。
1987.6 文部省在外研究員(甲、短期)派遣にて遺伝子発現制御に関する研究従事のため仏国パスツール研究所(Dr. A. Danchin)にて滞在研究(1ヶ月)とセミナー、その後、訪問教授として米国ユタ大学医学部生化学で研究に従事(1ヶ月)、フライブルク大学科学研究所Dr.Schulz)にてセミナー
1989.5 第6回国際アイソザイム会議(富山)にてセミナーに招待される(講演と発表)。
1991.5 米国カリフォルニア大学脂質研究所訪問、米国ユタ大学医学部生化学に短期滞在研究(2 ヶ月)
1991.8 韓国延世大学理学部蛋白研究所セミナーに招待される。
1994.3 国際シンポジウム-Dynamics in Biological Function of Adenylate Metabolism(防府)組織委員、並びにシンポジストとして講演
1995.6 春期韓国生化学会シンポジウムにて招待講演、漢陽大学、バイオサイエンスー
バイオテクノロジー研究所にてセミナー、延世大学理学部、タンパク質研究所にて講演
1995.6 第8回国際アイソザイム会議(フリフィス大、豪)にてシンポジストとして講演
1995.9 米国実験生物学会(ニューオーリンズ)にて発表、さらにJohns-Hopkins大学生化学にてセミナー講演
1995.10 第1回NM23/NDP Kinaseワークショップ(パスツール研究所)にて招待講演と発表
1995.11 第49回日本栄養食糧学会、西日本支部大会にて特別講演"脳と栄養"
(1985年より愛媛大学医学部、生化学、及び衛生学、さらに熊本大学医学部衛生学の非常勤講師を平成11年度まで務める)

2000年3月退官

2000年4月〜2003年3月阿波岐ヶ原病院

2003年4月より南九州大学健康栄養学部、管理養学科、教授(生化学担当)



1964. 9 日本生化学会(評議員)
1964. 9 日本ビタミン学会
1977. 1 日本衛生学会(評議員)
1985. 11 日本分子生物学会
1981 日本疫学会(評議員)
1988. 4 日本栄養食糧学会などの会員
1977. 4 American Chemical Society
1997. 9 American Society for Biochemistry and Molecular Biology,
1978. 4 Shigma Xi /The Scientific Research Societyの会員(加入年月は省略)



Bibliography
[1] Literary Work and review;


1. Jakoby W. B., Methods in Enzymology "Enzyme purification and relatedtechniques, Section V. Chromatographic procedures, (30). Preparation of calciumphosphate gel deposited on cellulose. (1971)

Koike M. and Hamada M., Academic Press, New York. Vol. XXII, pp.339-342.

2. Ogura et al., Molecular Mechanism of Enzyme Action Structure and actionmechanism of
α-keto acid dehydrogenase multienzyme complex. (1972)

Koike M., Hamada M., Koike K., Tanaka N., Ohtsuka K., and Suematsu T.,Tokyo University Press, Tokyo, pp. 197-215.
p
3. Markert C. L., Isozyme II. Physiological Functions of Relationship betweenthe Change in the Tertiary structure of Human Tumor Lactate Dehydrogenase andCarcinogenesis. (1975)

Hamada M., Academic Press, New York, pp. 143-156.

4. Gubler C. J. et al., Thiamine, 1. Thiamine depended Enzymes, Purification andFunction of
α-keto Acid Dehydrogenase in the Mammalian Multi-enyzme Complexes.

Kioke M., Hamada M., Koike K., Hiraoka T., and Nakaura Y. John WileySons, New York, pp. 5-13.

5. Lennon D.L.F. et al., Steenbock-Lilly Symposium on Biochemistry of MetabolicProcesses. Some Enzymic Studies on Human Duchenne Muscular Dystrophy. (1983)

Kuby S. A., Hamada M., Nesset C.C., Tyler F. H., and Ziter F.A., ElsvierBiomedical Inc., New York, pp. 303-322.

6. Schwartz S., Structure and Functions of SR Presteady state kinetics of E〜Pformation and decomposition by Ca, Mg-ATPase in bovine aorta microsomea. (1985)

Sumida M., Okuda H., Hamada M., Takenaka H., Waters J. M., Sarmiento J.G., and Froelich J. P., Academic Press Inc., New York pp. 297-303.

7. Markert C. L. et al., Isoenzymes. Structure and Function of Adenylate KinaseIsozymes in Normal Humans and Muscular Dystrophy Patients. (1988)

Hamada M., Sumida M., Kurokawa Y., Takenaka H., Fukamachi S., FumumotoK., Yamaguchi T., and Kuby S. A., Allan R. Liss Inc., Vol. 16, pp.81-108.

8. Kuby S.A., A Study of Enzymes, Structure and Mechanism of Enzyme Action: AStudy from Selected Examples, Chapter 8. Phosphotransferase, b. AdenylateKinase. (1991)

Hamada M. Takenaka H., Sumida M., and Kuby S. A., CRC Press, Boca Raton,Florida, Vol. II pp. 403-444.

9. Kuby S.A., A Study of Enzymes, Structure and Mechanism of Enzyme Action: AStudy from Selected Examples, Chapter 9. Dehydrogenase, c. 2-Oxo aciddehydrogenases. (1991)

Hamada M.
and Takenaka H., CRC Press, Boca Raton, Florida, Vol. II pp.227-245.

10. Kuby S. A., A Study of Enzymes, Structure and Mechanism of Enzyme Action: AStudy from Selected Examples, Chapter 14. a. Ca2+, Mg2+-ATPase (Microsomal).(1991)

Takenaka H., Hamada M., and Sumida M., CRC Press, Boca Raton, Florida,Vol. II pp. 345-365.

11. Recent Development in Biochemistry. The Reaction Mechanism of HumanAdenylate Kinase. The Steady-State Kinetics of the Mutants Constructed byProtein Engineering of Site-Directed Mutagenesis. (2000)

Ayabe T and Hamada M., Research Signpost, Kerara (in press)

12. Claret L., The Encyclopedia of Molecular Medicine Adenylate Kinase (Human)(2000)


Ayabe T. and Hamada M., John Wiley & Sons, Inc., New York (in press)

(他、邦文の分担執筆やレビュー誌 18編、計30編)

Publication:

1. Mammalian
α-keto acid dehydrogenase complexes, 1. Isolation, purificationand properties of pyruvate dehydrogenase complex of pig heart muscle. HayakawaT., Hirashima M., Ide S., Hamada M., Okabe K., and Koike M., J. Biol.Chem., 241, pp. 4694- 4699 (1966)
2. Effect of various bivalent cations and chelating agents on the oxidative decarboxylationof
α-keto acids. Hayakawa T., Hirashima M., Hamada M., and Kioke M.,Biochem. Biophys. Acta, 128, pp. 574-576 (1966)
3. Purification and Comparative properties of human lactate dehydrogenaseisozymes from uterus, uterine myoma and cervical cancer. Okabe K., Hayakawa T.,Hamada M., and Koike M., Biochemistry, 7, pp. 79-90 (1968)
4. Mammalian
α-keto acid deydrogenase complexes, IV. Substrate specificitiesand kinetic properties of the pig heart pyruvate and 2-oxoglutarate dehydrogenasecomplexes. Kanzaki T., Hayakawa T., Hamada M., Fukuyoshi Y., and KoikeK., J. Biol. Chem., 244, pp. 1183- 1187 (1969)
5. Function of thiamin diphosphate in oxidative decarboxylation of
α-ketoacids. Koike M., Hamada M., and Tanizaki T., J. Nutr. Sci., 15, pp.325-326 (1969)
6. Effect of thiamin triphosphate on
α-keto acid dehydrogenase and pyruvate. HamadaM., J. Nutr. Sci., 15, pp. 325-326 (1969)
7. Mammalian
α-keto acid dehydrogenase complexes, VI. Nature of the multipleforms of pig heart lipoamide dehydrogenase. Sakurai Y., Fukuyoshi Y., HamadaM., Hayakawa T., and Koike K., J. Biol. Chem., 245, pp.4453-4462 (1970)
8. Rsolution and reconstitution of pig heart 2-oxoglutarate dehydrogenasecomplex. Kioke K., Tanaka N., Hamada M., Ohtsuka T., Sueamtsu T., andKoike M., J. Biochem., 69, pp. 1143- 1147 (1971)
10. Mammalian
α-keto acid dehydrogenase complexes, VII. Resolution andreconstitution of the pig heart lipoate succinyltransferase. Tanaka N., KoikeK., Hamada M., K. Ogasahara K., and Koike M., J. Biol. Chem., 249, pp.4043-4049 (1972)
11. Mammalian
α-keto acid dehydrogenase complexes, VIII. Properties and subunitcomposition of the pig heart lipoate succinyltransferase. Tanaka N., Koike K., HamadaM., K. Ogasahara K., and Koike M., J. Biol. Chem., 249, pp. 191-198 (1974)
12. Properties and subunit composition of the pig heart 2-oxoglutaratedehydrogenase. Kioke K., Hamada M., Tanaka N., Ogasahara K., and KiokeM., J. Biol. Chem., 249, pp. 3836- 3842. (1974)
13. Experimental infection with myocoplasma pneumonia in the young hamsterlocation of ferritin-labeled antibody binding to infective tissue. Hara K.,Izumikawa K., Kinoshita I., Ohta M., Ikebe A., Koike M., and Hamada M.,Tohoku J. Exp., 114, pp. 315-337 (1975)
14. Kinetic study of the
α-keto acid dehydrogenase complexes from pig heartmitochondria. Hamada M., Kioke K., Nakaura Y., Hiraoka T., Kioke M., andT. Hashimoto T., J. Biochem., 77, pp. 1047-1056 (1975)
15. Purification, properties and subunit composition of the pig heart lipoaeacetyltransferase. Hamada M., Ohtsuka K., Tanaka N., Ogasahara K., KoikeK., Hiraoka T., and Koike M., J. Biochem., 78, pp. 187-197 (1975)
16. Effect of guanidine hydrochloride on the holo- and apoenzymes of pig heartlipoamide dehydrogenase. Ogasahawa K., Koike K., Hamada M., and KoikeM., J. Biochem., 79, pp. 819-828 (1976)
17. Interaction of hydrophobic probes with the apoenzymes of the pig heartlipoamide dehydrogenase. Ogashara K., Kioke K., Hamada M., and Koike M.,J. Biochem., 79, pp. 967-975 (1976)
18. ATP-AMP trasnferase (Myokinase) from rabbit and calf muscle, Structure andEquilibrium Binding. Kuby S.A., Hamada M., Palmieri R.H., Tsai W.C.,Jacobs H. K., Maland, L., Wu L., and Fisher A., Fed. Proc. 35, pp. 1629 (1976)
19. Properties and subunit structure of pig heart pyruvate dehydrogenase. HamadaM., Hiraoka T., Koike K., Ogasawara K., Kanzaki T., and Koike M.., J.Biochem., 79, pp. 1273-1285 (1977)
20. Studies on adenosine triphosphate transphosphorylase XII. Isolation andseveral properties of the crystalline calf ATP-AMP transphosphorylase(adenylate kinase) from muscle and liver and some observations on the rabbitmuscle adenylate kinases. Kuby S. A., Hamada M., Gerber D., Tsai W. C.,Jacobs, H.K., Cress, M.C., Chua G. H., Fleming G., Wu L., Frishat A., AndMaland L., Arch. Biochem. Biophys., 190, pp. 772-792 (1978)
21. Studies on adenosine triphosphate transphosphorylase (adenylate kinase) anda comparison with the crystalline calf muscle liver adenylate kinase. HamadaM. and Kuby S. A., Arch. Biochem. Biophys., 190, pp. 772-792 (1978)
22. Studies on adenosine triphosphate transphosphorylase XIV. Equilibriumbinding properties of the crystalline rabbit and calf muscle ATP-AMPtransphophorylase (adenylate kinase) and derived peptide fragments. HamadaM., Palmieri R. H., Russel G. H., and Kuby S. A., Arch. Biochem. Biophys.,195, pp. 155-177 (1981)
23. Studies on NADH-cytochrome c reductase I. Isolation and several propertiesof the crystalline enzyme from ale yeast. Tryon E., Cress M.C., Hamada M.,and Kuby S.A., Arch. Biochem. Biophys., 197, pp. 104-118 (1981)
24. An aberrant adenylate kinase isozyme from the serum of patients withDuchenne muscular dystrophy. Hamada M., Okuda H., Oka T., Watnabe T.,Ueda K., Nojima M., Kuby S. A., Manship M., Tyler F., and Ziter F., Biochem.Biophys. Acta, 660, pp. 227-237 (1981)
25. Human isoenzymes of adenylate kinase and physicochemical comparison of thenormal human enzymes with the aberrant adenylate kinase from Duchennedystrophic serum. Hamada M., Sumida M., Okuda H., Watanabe T., NojimaM., and Kuby S.A., Fed. Proc. Abstr. 41, pp.903 (1982)
26. Adenosine triphosphate-adenosine 5-monophosphate phosphotransferase fromnormal human liver mitochondria. Isolation, chemical properties andimmunochemical comparison with Duchenne dystrophic serum aberrant adenylatekinase. Hamada M., Sumida M., Okuda H., Watanabe T., Nojima M., and KubyS.A., J. Biol. Chem., 257, pp. 13120-13128 (1982)
27. Effect of lipolytic and anti-lipolytic hormones on perfused rat fat cells.Sumida M., Hamada M., Nagai K., and Okuda H., Biomed. Res., 3, pp.590-598(1982)
28. Studies on adenosine triphosphate transphophorylase XV. Human isoenzymes ofadenylate kinase. Isolation and physio-chemical comparison of the crystallinehuman ATP-AMP transphosphorylase from muscle and liver. Kuby S. A., Fleming G.,Frishat A., Cress M.C., and Hamada M., J. Biol. Chem., 258, pp.1910-1907 (1984)
29. Ca2+, Mg2+-ATPase of microsomal membranes and from bovine aortic smoothmuscle. Identification and characterization of an acid-stable phophorylatedintermediate of the Ca2+, Mg2+-ATPase. Sumida M., Okuda H., and Hamada M.,J. Biochem., 96, pp. 1365-1374 (1984)
30. Studies on the adenylate kinase isozymes from the serum and erythrocyte ofnormal and Duchenne dystrophic patients. Isolation, physico-chemical propertiesand several comparisons with the Duchenne dystrophic aberrant enzyme. HamadaM., Sumida M., Kurokawa Y., Sunayoshiki-Kusuzaki K., Okuda H., Watanabe T.,Kuby S. A., J. Biol. Chem., 260, pp.11595-11602 (1985)
31. Ca2+, Mg2+-ATPase of microsomal Membranes from Bovine Aortic Smooth MuscleEffects of Sr2+, Cd2+ on Ca2+ uptake and Formation of PhosphorylatedIntermediate of the Ca2+, Mg2+-ATPase. Sumida M., Hamada M., TakenakaH., Hirata Y., Nishigauchi K., and Okuda H., J. Biochem., 100, pp. 765-772(1986)
32. Ca2+ uptake in bovine adrenocortical microsomes formation of phosphorylatedintermediate for Ca2+-ATPase. Sumida M., Hamada M., Shiosaka K.,Morimoto C., and Okuda H., J. Biochem., 104, pp. 687-692 (1988)
33. Axonal transport in mdx mouse sciatic nerve. Yamashita S., Takenaka H.,Sugimoto S., Chihara E., Matsukura S., and Hamada M., J. Neurol. Sci.,92, pp.267-279 (1989)
34. Effects of prolonged hypothermic ischaemia on calcium transport by myocardialsacroplasmic reticulum. Fukumoto K., Takenaka H., Koga Y., and Hamada M.,Cardiovascular Res., 24, pp. 169-175 (1989)
35. Synthetic genes for human muscle-type adenylate kinase in Escherichia Coli.Kim H.J., Nishikawa S., Tanaka T., Uesugi S., Takenaka H., Hamada M.,and Kuby S.A., Protein Engineering, 2., pp. 379-386 (1989)
36. Studies on adenosine Triphosphate Transphosphorylase XVIII. Synthesis andpreparation of peptides and peptide fragments of rabbit muscle: ATP-AMPtransphosphrylase (adenylate kinase) and their nucleotide binding properties.Kuby S.A., Hamada M., Johnson M.S., Russel G.A.; Manship M., R.H.,Palmieri G., Fleming G., Bredt D., and Mildvan A.S., J. Prot. Chem., 8, pp.549-562 (1989)
37. In Vitro Mutagenesis studies at the arginine residues of adenylate kinase.A revised binding site for AMP in the X-ray deduced model. Kim H.J., NishikawaS., Tokutomi Y., Takenaka H., Hamada M., Kuby S.A., and Uesugi S.,Biochemistry, 29, pp. 1107-1111 (1990)
38. Multiforms of mammalian adenylate kinase and its monoclonal antibodyagainst AK1. Kurokawa Y., Takenaka H., Sumida M., Oka K., Hamada M., andKuby S.A., Enzymes, 43, pp. 57-71 (1990)
39. kinetic properties and isozyme composition of myosin in the mdx mutantmouse. Sugimoto S., Takenaka H., Yamashita S., Matsukura S., and Hamada M.,J. Neurol. Sci., 97, pp. 207- 219 (1990)
40. Bisdiamine induced teratogenesis for rat embryo. Tasaka H., Takenaka H.,Okamoto N., Koga Y., and Hamada M., Teratology 42, pp. 25A (1990)
41. Effect of hypothermic ischaemia and reperfusion on calcium transport bymyocardial sarcolemma and sarcoplasmic reticulum. Fukumoto K., Takenaka H.,Koga Y., and Hamada M., J. Mol. Cell. Cardiol., 23, pp. 525-535 (1990)
42. Characterization of Magnesium dependent adenosine 5'-triphosphatein bovinebrian cytoplasmic dynein. Yamashita S., Takenaka H., Sugimoto S., Chihara E.,Sawada A., Matsukura S., and Hamada M., Biochemistry Intl., 22, pp.815-820 (1991)
43. Characterization of the Seady-State Mg2+Dependent Adenosine 5-triphosphataseof Bovine Brain kinesin in the Absence of Microtubles. Yamashita S., TakenakaH., Chihara E., Sugimoto S., Matsukura S., Sawada A., and Hamada M., J.Clin. Biochem. Nutr., 10, pp. 1- 14 (1991)
44. Diaphragmatic Hernia Induced in Rat Fetuses by Administration ofBisdiamine. Tasaka H., Takenaka H., Okamoto N., Koga Y., and Hamada M..,Cong. Anom., 32, pp. 347-355 (1992)
45. Atroventricular Septal Defect in Rat Fetuses induced by Aministration ofBisdiamine. Tasaka H., Okamoto N., Takenaka H., Koga Y., and Hamada M., Cong.Anom., 33, pp. 31- 44 (1993)
46. Caridioplegic effect of University of Wisconsin solution on hypothermicischaemia of rat myocaridium assessed by mitochondrial oxidativephosphorylation. Yano H., Takenaka H., Onitsuka T., Koga Y., and Hamada M..,J. Thor. Cardiovasc. Surg., 106, pp. 502-510 (1993)
47. Construction of the Plasmid pMEX8-hAK1 and Random Site-Directed Mutagenesisof Human Adenylate Cytosolic Adenylate Kinase. Ayabe T., Takenaka H., TakenakaO., Takenaka A., Nagahama H., Maruyama H., Yamamoto A., Nagata M., Koga Y.,Sumida M., and Hamada M., Biochem. Mol. Biol. Int. 38, pp. 373-381(1996)
48. Catalytic Roles of Lysines (K9, K27, K31) in the N-terminal Domain in HumanAdenylate Kinase by Random Site-Directed Mutagenesis. Ayabe T., Park S.K.,Takenaka H., Sumida M., Uesugi S., Takenaka O., and Hamada M., Biochem.Mol. Biol. Int. 40, pp. 879-909 (1996)
49. Protection of Isolated Lung from reperfusion Injuries by Rinsing with HighColloidal Osmotic Solution with Deferoxamine. Shibuya K., Edagawa M., TakenakaH., Matsuzaki Y., Shibata K., Onitsuka T., Koga Y., and Hamada M.,Transplantation, 62, pp. 179-185 (1996)
50. Protective Effects of
α-Tocopherol against Glucose Intolerance andMitochondrial Damage in Perfused Rat Liver. Maruyama H., Takenaka H., HayashiK., Maruyama T., Tsubouchi H., Kuwabara M., and Hamada M., J. Clin.Biochem. Nutr. 21, pp. 191-207 (1996)
51. Steady-State Kinetics of Thr35 and Thr39 Mutants in Human Adenylate Kinaseby Site- Directed Mutagenesis. Ayabe T., Takenaka H., Onitsuka T., Shibata K.,Takenaka O., Uesugi S., and Hamada M., Enzyme & Protein, 49, pp.305-312 (1996)
52. Essential Lysine Residues in the N-terminal and the C-terminal Domain ofHuman Adenylate Kinase Interact with Adenine Nucleotides as found bySite-Directed Random Mutagenesis. Ayabe T., Takenaka H., Takenaka O., SumidaM., Maruyama H., Onitsuka T., Shibata K., Uesugi S., and Hamada M.,Biochemistry, 36, pp. 4027-4033 (1997)
53. Substrate-Binding and Catalytic roles of Lys194 in the C-terminus in HumanAdenylate Kinase by Site-Directed Random Mutagenesis. Ayabe T., Takenaka H.,Takenaka O., Onitsuka T., Shibata K., Uesugi S., and Hamada M., Biochem.Mol. Biol. Int., 41, pp. 367- 375 (1997)
54. Suppression of Reperfusion Injury in Rat Skeletal Muscle by AntioxidativeEnzymes. Yamamoto A., Takenaka H., Shibata K., Onitsuka T., Koga Y., and HamadaM., J. Clin. Biochem. Nutr., 23, pp. 53-67 (1997)
55. Effect of Prolonged Hypothermic Ischaemia and Reperfusion on OxygenConsumption and Total Mechanical Energy in Rat Myocardium. Kuwabara M.,Takenaka H., Maruyama H., Onitsuka T., and Hamada M., Transplantation,64, pp. 577-583 (1997)
56. The comparison of simultaneous changes of serum magnesium and potassium inpatients with various diseases. Saito N., Nagatomo H., Sakurai H., Nakajima I.,Murata T., Yasunaga Y., Nakayama S., Kamitani M., Suzuku A., Sayama H., HamadaM., and Kannagi T., Jpn. J. S. Mg. Res., 16, pp. 123-135 (1997)
57. Comparison between colorimetry with xylidyl blue blue and atomic absorptionspectrophotoscopy in measuring serum magnesium level. Saito N., Nakayama S.,Kamitani M., and Hamada M., Jpn. J. S. Mg. Res., 16, pp. 137-146 (1997)
58. Site-Directed Mutagenesis and Steady-State Kinetic Analysis of Mutant Enzymesof Human Adenylate Kinase., Ayabe T., Park S. K., Nagahama H., Maruyama H.,Sumida M., Takenaka H., Takenaka O., Onitsuka T., and Hamada M. Biochem.Mol. Biol. Int., 46, pp. 673-680 (1998)

(他 省略の92編、計150編)


学会発表

1. Human tumor lactate dehydrogenase and carcinogenasis. Hamada M., The3rd International Conference on Isozymes, (Yale) (1975)
2. Nature of the multiple forms of pig heart lipoamide dehydrogenase. HamadaM., The 3rd. International Conference on Isozymes, (Yale) (1975)
3. ATP-AMP Transphosphorylase (Myokinase) from rabbit and calf muscle:Structure and equilibrium binding, Kuby S. A., Hamada M., Palmieri R.H., Tsai W. C., Jacobs H.K., Maland L., Wu L., and Fisher A., Fed. Proc.(FASEB) (San Fransisco) (1977)
4. Kinetic properties of the rabbit muscle ATP^AMP transphosphorylase andcomparison with the crystalline calf muscle and liver adenylate kinase. Kuby S.A., Hamada M., Palmieri R. H., Cress M.C., Fleming G., and Maland L.,Fed. Proc., (FASEB) (NewOrleanse) (1982)
5. Human ATP-AMP transphosphorylase (Adenylate kinase)-structure and itsfunction. Hamada M., Sumida M., Okuda H., Watanabe T., and Nojima M.,Fed. Proc., (FASEB) (NewOrleanse) (1982)
6. Human Adenylate Kinase Isozymes-Structure and Function. Hamada M.,5th International Conference on Isozymes, (Cos) (1986)
7. Protein Engineering of Human Adenylate Kinase Isozymes. Hamada M.,Takenaka H., Kim H. J., Nishikawa S., and Uesugi S., 6th InternationalConference on Isozymes, (Toyama) (1988)
8. Adenylate Kinase-structure and function. Hamada M., Protein ResearchCenter Seminar, Yonsei Univ., (Seoul)(1991)
9. Protein Engineering of Human Adenylate Kinase. Hamada M., Ayabe T.,Takenaka H., and Uesugi S., International Symposium: Dynamics in BiologicalFunction of Adenylate Metabolism, (Houhu) (1994)
10. Site-Directed mutagenesis and Functional Analysis of the active SiteResidues (K21, K27, and T39) of Human Adenylate Kinase. Hamada M., AyabeT., and Takenaka H., 8th International Congress on Isozymes (Gene Families:Structure, Function, Genetics and Evolution) (Brisbane) (1995)
11. Essential Key Lysine Residues (K9, K21, K27, K31, and K194) at MgATPBinding Site in N- and C-terminus Domain of Human Adenylate Kinase (AK1). HamadaM., Ayabe T., Takenaka H, Takenaka O., Maruyama H., Nagata M., Nagahama H.,Yamamoto A., And Koga Y., First International Workshop on nm23/NDP Kinase,(Paris) (1995)
12. Phosphotransferase-Structure and Mechanism of Adenylate Kinase. HamadaM.., Ayabe T., and Takenaka H., '96 Spring Science Meet & GeneralAssembly, Symposium (Soul) (1996)
13. General Features of Adenylate Kinase, Structure and its Engineered Mutants.Hamada M., Korea Research Institute of Bioscience and Biotechnology(HIST), Seminar, (Daejeon) (1996)
14. A Rapid and effective Site-Directed Mutagenesis with specific PrimerAnnealing to Single strand pMEX8-hAK. Hamada M., Bio-Product ResearchCenter, Symposium Yonsei. Univ. (Seoul)(1996)
15. Site-Directed Mutagenesis and Functional Analysis of Active Site Residues(K21, K27, T35) of Human Adenylate Kinase. Hamada M., College of ScienceSeminar, Hang Yang Univ. (Ansan) (1996)
16. Structure ad Mechanism of Human adenylate Kinase: Site-Directed Mutagenesisand Functional Analysis of the Active Site Residues. Hamada M., Dept.Biol. Chem., Seminar, Johns Hopkins Univ. (Baltimore) (1996)
17. The relationship between serum magnesium and aging or magnesium oxideadministration. Saito N., Doi Y., Aomi H., Nakajima I., Murata T., Yasunaga Y.,Tsutsumi, T., Nakayama M., Kamitani M., Sayama T., Kannagi T., and Hamada M.,The 16th Congress of international Asociation of Gerontology (Adelaide)(1977)
18. The Comparisons among magnesium measurements through various methods. SaitoN., Nakayama M., Kamitani M., and Hamada M., The VIII InternationalSymposium on Magnesium (Heraklion)(1997)

(以上、国際学会における主たるもの、18編、ほか全国レベルのもの5編)