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1. Kazuo Yamasaki,
Takashi Daiho, and Hiroshi Suzuki.
Remarkable
Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase
with Tightly Bound Fluoride and Magnesium against Detergent-induced
Denaturation.J.
Biol. Chem.
in press, 2002
2. Stefania Danko, Kazuo Yamasaki,
Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
Organization
of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase
in E1P and E1ATP states: a limited proteolysis study.
FEBS
Letters, Vol.505, 129-135, 2001
(Hiroshi
Suzuki; corresponding author)
3. Takashi Daiho,
Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime
Iizuka,andHiroshi Suzuki.
Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum
Ca2+-ATPase Resultin a Complete Loss of Ca2+Transport
Activity without a Loss of
Ca2+-ATPase
activity.J. Biol. Chem.Vol.276(35), 32771-32778, 2001
4. Hidetoshi Takahashi,
Yoshiaki Atsuta, Katsuhiko Sato, Akemi Ishida-Yamamoto, Hiroshi Suzuki,
and Hajime Iizuka.
Novel mutations of ATP2A2 gene in Japanese patients of Darier's disease.
J.
Dermatol. Sci. Vol.26(3), 169-172, 2001
5. —é–Ø@—TBCa2+ƒ|ƒ“ƒvBƒVƒŠ[ƒYEƒoƒCƒIƒTƒCƒGƒ“ƒX‚ÌV¢‹I
Vol.12uŠ´ŠoŠíН‚Æ”]“àî•ñˆ—vi“ú–{¶‰»Šw‰ïE‹¤—§o”ÅjAˆóü’†A2001
6. —é–Ø@—TBœŠi‹Ø‚ÌŽûkE’oŠÉ‚̃XƒCƒbƒ`‚͉½‚©H\\‹»•±Žûk˜AŠÖB‰^“®‚Æ•ªŽq¶•¨ŠwQ&A(‘åCŠÙ‘“X)Aˆóü’†A2001
7. Stefania Danko,
Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi
Toyoshima.
ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase
has a compact conformation resistant to proteinase K, V8 protease and trypsin.
FEBS Letters, Vol.498(2-3), 277-282,
2001 (Hiroshi Suzuki; corresponding author)
8. Hiroshi Suzuki,
Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Only half of the Ca2+-ATPase molecules present in sarcoplasmic
reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
in Na/K-ATPase and Related ATPases. (K.Taniguchi and S.Kaya Eds.) pp.381-388,
2000, Elsevier, North Holland,
9. Takashi Daiho,
Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or specific substitutions of a few residents in the NH2-terminal
Ala3-Thr9 region of sarcoplasmic reticulum Ca2+-ATPase cause
inactivation and rapid degradation of
the enzyme expressed in COS-1 cells.
in Na/K-ATPase and Related ATPases.
(K.Taniguchi and S.Kaya Eds.) pp.293-296, 2000, Elsevier, North Holland,
10. Kazuo Yamasaki, Takashi
Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations ofarginine-198 in sarcoplasmic reticulum Ca2+-ATPase
cause inhibition of hydrolysis of the phosphoenzyme intermediate formed
from inorganic phosphate.
in Na/K-ATPase and Related ATPases. (K.Taniguchi and S.Kaya Eds.) pp.297-300,
2000, Elsevier, North Holland,
11. Takashi Daiho, Kazuo
Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or Specific Substitutions of a Few Residues in the NH2-terminal
Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inactivation and Rapid
Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem.
Vol.274(34),
23910-23915, 1999
12. Takashi Daiho, Hiroshi
Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from
Inorganic Phosphate.
FEBS Letters Vol. 444(1), 54-58, 1999
13. Hiroshi Suzuki and
Tohru Kanazawa.
Formation of the ADP-Insensitive Phosphoenzyme Intermediate in the Sarcoplasmic
Reticulum Ca2+-ATPase of Which both Cys344 and Cys364 Are Modified
by
N-Ethylmaleimide.
Biochemistry
Vol.38 (2), 820-825, 1999
14. —é–Ø@—TBCa2+ƒ|ƒ“ƒv\\Œ`Ž¿–Œ‚Ƭ–E‘ÌB’`”’Ž¿ŠjŽ_y‘fVol.43
(10)i‘Ч†FƒJƒ‹ƒVƒEƒ€‚ƃVƒOƒiƒ‹“`’BjA1610-1621A1998
15. Satoshi Nakamura, Hiroshi
Suzuki and Tohru Kanazawa.
Stoichiometry of Phosphorylation to Fluorescein 5-Isothiocyanate Binding
in the Ca2+-ATPase of Sarcoplasmic Reticulum Vesicles.
J. Biol. Chem. Vol.272 (10), 6232-6237, 1997
16. Keisuke Kimura, Hiroshi
Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic
Reticulum Ca2+-ATPase: Modification with 1,2-Cyclohexanedione.
J. Biol. Chem. Vol.271 (46), 28933-28941, 1996
17. Hiroshi Suzuki and
Tohru Kanazawa.
Reduction in Water Activity Greatly Retards the Phosphoryl Transfer from
ATP to Enzyme Protein in the Catalytic Cycle of Sarcoplasmic Reticulum
Ca2+-ATPase.
J. Biol. Chem. Vol.271 (10), 5481-5486, 1996
18. Tohru Kanazawa, Hiroshi
Suzuki, Takashi Daiho, and Kazuo Yamasaki.
Fluorometric Study on Conformational Changes in the Catalytic Cycle of
Sarcoplasmic Reticulum Ca2+-ATPase.
Bioscience Reports
Vol.15 (5), 317-326, 1995
19. Hiroshi Suzuki and
Tohru Kanazawa.
The Tryptophan Fluorescence Change upon Conformational Transition of the
Phosphoenzyme Intermediate in Sarcoplasmic Reticulum Ca2+-ATPase
Is Revealed in the
Absence of K{and the Presence of Lasalocid.
J. Biol.
Chem. Vol.270 (7), 3089-3093, 1995
20. Hiroshi Suzuki, Satoshi
Nakamura, and Tohru Kanazawa.
Effects of Divalent Cations Bound to the Catalytic Site on ATP-Induced
Conformational Changes in the Sarcoplasmic Reticulum Ca2+-ATPase:
Stopped-Flow Analysis of the
Fluorescence of N-Acetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine Attached
to Cysteine-674. Biochemistry
Vol.33 (27), 8240-8246, 1994
21. Satoshi Nakamura, Hiroshi
Suzuki, and Tohru Kanazawa.
The ATP-induced Change of Tryptophan Fluorescence Reflects a Conformational
Change upon Formation of ADP-sensitive Phosphoenzyme in the Sarcoplasmic
Reticulum
Ca2+-ATPase: Stopped-Flow Spectrofluorometry and Continuous
Flow-Rapid Quenching Method. J. Biol. Chem. Vol.269 (23),
16015-16019, 1994
22. —é–Ø@—TB‹Ø¬–E‘ÌCa2+-ATPƒA[ƒ[B¶‰»ŠwA‘æ64Šªi‘æ12†jA1444-1449A1992
23. Hiroshi Suzuki, Tatsuya
Kubota, Koji Kubo, and Tohru Kanazawa.
Existence of a Low-affinity ATP-binding Site in the Unphosphorylated Ca2+-ATPase
of Sarcoplasmic Reticulum Vesicles: Evidence from Bionding of
2',3'-0-(2,4,6-Trinitrocyclohexandienylidene)-[3H]AMP and -[3H]
ATP. Biochemistry Vol.29 (30), 7040-7045, 1990
24. Koji Kubo, Hiroshi
Suzuki, and Tohru Kanazawa.
Characterization of the Substrate-induced Conformational Change of N-Iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine-lebeled
Sarcoplasamic Reticulum Ca2+-ATPase
by Using Different Kinds of Substrate.Biochimi. Biophys. Acta Vol.1040(2),
251-259, 1990
25. Hiroshi Suzuki, Mitsuhiro
Obara, Koji Kubo, and Tohru Kanazawa.
Changes in the Steady-state Fluorescence Anisotropy of N-Iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
Attached to the Specific Thiol of Sarcoplasmic Reticulum
Ca2+-ATPase throughout the Catalytic Cycle.J. Biol. Chem.
Vol.264 (2), 920-927, 1989
26. Hiroshi Suzuki, Yoshifusa
Kondo, Aida D. Carlos, and John C. Seidel.
Effects of Phosphorylation, MgATP, and Ionic Strength on the Rates of Papain
Degradation of Heavy and Light Chains of Smooth Muscle Heavy Meromyosin
at the
S1-S2 Junction. J. Biol. Chem. Vol.263 (22), 10974-10979,
1988
27. Mithsuhiro Obara, Hiroshi
Suzuki, and Tohru Kanazawa.
Conformational Changes in the Vicinity of the N-Iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
Attached to the Specific Thiol of Sarcoplasmic Reticulum Ca2+-ATPase
throughout the Catalytic Cycle.J. Biol. Chem. Vol.263 (8),
3690-3697, 1988
28. Hiroshi Suzuki, Mitsuhiro
Obara, Hideto Kuwayama, and Tohru Kanazawa.
Conformational Changes in the Vicinity of the N-Iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
Attached to the Specific Thiol of Sarcoplasmic Reticulum Ca2+-ATPase
through the Catalytic Cycle.Calcium Signal and Cell Response
(K. Yagi and T. Miyazaki Eds.) 332-334, 1988
29. Hiroshi Suzuki, Mitsuhiro
Obara, Hideto Kuwayama, and Tohru Kanazawa.
A Conformational Change of N-Iodoacetyl-N'-(5-sulfo-1-naphthyul)ethylenediamine-labeled
Sarcoplasmic Reticulum Ca2+-ATPase upon ATP Binding to the Catalytic
Site.
J. Biol. Chem. Vol.262 (32), 15448-15456, 1987
30. Sumitra Nag, Hiroshi
Suzuki, Jan Sosinski, and John C. Seidel.
Conformational Changes in Myosin and Heavy Meromyosin from Chicken Gizzard
Associated with Phosphorylation.
Regulation and Contraction of Smooth Muscle (Siegman, M. J., Somlyo,
A. P., and Stephens, N. L. Eds.) Vol.91-108,
1987
31. Hiroshi Suzuki, Walter
F. Stafford, III, Henry S. Slayter, and John C. Seidel.
A Conformational Transition in Gizzard Heavy Meromyosin Involving the Head-Tail
Junction, Resulting in Changes in Sedimentation Coefficient, ATPase Activity,
and
Orientation of Heads.J. Biol. Chem. Vol.260, 14810-14817,
1985
32. T. S. Chandra, Narindar
Nath, Hiroshi Suzuki, and John C. Seidel.
Modification of Thiols of Gizzard Myosin Alters ATPase Activity, Stability
of Myosin Filaments, and the 6-10S Conformational Transition.
J. Biol.Chem.
Vol.260, 202-207, 1985
33. —é–Ø@—TB•½ŠŠ‹ØŽûk§Œä‚Ì•ªŽq‹@\|Œy½‚ÌƒŠƒ“Ž_‰»‚È‚ç‚тɒEƒŠƒ“Ž_‰»‚É‚æ‚éƒ~ƒIƒVƒ“•ªŽq‚ÌŒ`‘ԕω»|BŒŒŠÇu–¬ŠÇŒ¤‹†vA6ŠªA157-169A1983
34. Hiroshi Suzuki, Toshio
Kamata, Hirofumi Onishi, and Shizuo Watanabe.
Adenosine Triphosphate-Induced Reversible Change in the Conformation of
Chicken Gizzard Myosin and Heavy Meromyosin. J. Biochem.Vol.91,
1699-1705, 1982
35. Hiroshi Suzuki, Koui
Takahashi, Hirofumi Onishi, and Shizuo Watanabe.
Reversible Changes in the State of Phosphorylation of Gizzard Myosin, in
That of Gizzard Myosin Assembly, in the ATPase Activity of Gizzard Myosin,
in That of Actomyosin
and in the Superprecipitation Activity. J. Biochem.Vol.91,
1687-1698, 1982
36. Hiroshi Suzuki, Sawako
Suzuki, and Shizuo Watanabe.
High Concentrations of Magnesium for Formation of Thick-Filaments of Chicken
Gizzard Myosin.J. Biochem. Vol.89, 871-878, 1981
37. Hiroshi Suzuki, Kunihiko
Konno, Ken-ichi Arai, and Shizuo Watanabe.
ATP-Induced Tension Development in Glycerinated Fibers of Scallop Adductor
Striated Muscle: Role of Regulatory Light Chain of Myosin in Calcium Regulation
of Muscle
Contraction.J. Biochem.Vol.88, 909-911, 1980
38. Hiroshi Suzuki, Hirofumi
Onishi, Koui Takahashi, and Shizuo Watanabe.
Structure and Function of Chicken Gizzard Myosin. J. Biochem. Vol.84,
1529-1542, 1978
39. Hiroshi Suzuki, Kayoko
Nakamura, Koui Takahashi, and Shizuo Watanabe.
Adenosine Triphosphatase Activity and "Thick Filament" Formation of Chicken
Gizzard Myosin in Low Salt Media.
J. Biochem. Vol.83, 835-847,
1978
40. Hirofumi Onishi, Yoosuke
Yamada, Mitsuo Ikebe, Hiroshi Suzuki, and Shizuo Watanabe.
The ATPase Reaction in the Steady State and in the Initial Burst Catalyzed
by Chicken Gizzard Myosin in 0.6 M KC1. J. Biochem. Vol.83,
129-135, 1978
‘å@•Û@@‹M@Žk
1. Kazuo Yamasaki,
Takashi Daiho, and Hiroshi Suzuki.
Remarkable
Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase
with Tightly Bound Fluoride and Magnesium against Detergent-induced
Denaturation.
J.
Biol. Chem. in press, 2002
2. Stefania Danko,
Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
Organization
of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase
in E1P and E1ATP states: a limited proteolysis study. FEBS
Letters, Vol.505, 129-135, 2001
3. Takashi Daiho,
Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime
Iizuka, and Hiroshi Suzuki.
Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum
Ca2+-ATPase Result in a Complete Loss of Ca2+ Transport
Activity without a Loss of
Ca2+-ATPase activity, J. Biol. Chem. Vol.276(35),
32771-32778, 2001
4. Stefania Danko,
Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi
Toyoshima.
ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase
has a compact conformation resistant to proteinase K, V8 protease and trypsin.
FEBS Letters, Vol. 498(2-3), 277-282, 2001
5. Hiroshi Suzuki,
Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Only half of the Ca2+-ATPase molecules present in sarcoplasmic
reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier,
North Holland, 381-388, 2000
6. Takashi Daiho,
Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or specific substitutions of a few residents in the NH2-terminal
Ala3-Thr9 region of sarcoprasmic reticulum Ca2+-ATPase cause
inactivation and rapid degradation
of the enzyme expressed in COS-1 cells. Na/K-ATPase and Related ATPases.(K.Taniguchi
and S.Kaya Eds.)Elsevier, North Holland, 293-296, 2000
7. Kazuo Yamasaki,
Takashi Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations of arginine-198 in sarcoplasmic reticulum Ca2+-ATPase
cause inhibition of hydrolysis of the phosphoenzyme intermediate formed
from inorganic phosphate.
Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier,
North Holland,
297-300, 2000
8. Takashi Daiho,
Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or Specific Substitutions of a Few Residues in the NH2-terminal
Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inactivation and Rapid
Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem.
Vol.274
(34), 23910-23915, 1999
9. Takashi Daiho,
Hiroshi Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from
Inorganic Phosphate.
FEBS Letters Vol. 444 (1), 54-58, 1999
10. Kazuo Yamasaki, Takashi
Daiho, Tomoyuki Saino, and Tohru Kanazawa.
Modification of Histidine 5 in Sarcoplasmic Reticulum Ca2+-ATPase
by Dietyl Pyrocarbonate Causes Strong Inhibition of Formation of Phosphoenzyme
Intermediate from
Inorganic Phosphate.
J. Biol. Chem. Vol.272 (49), 30627-30636,
1997
11. Tomoyuki Saino, Takashi
Daiho, and Tohru Kanazawa.
Modification of Arginine-198 in Sarcoplasmic Reticulum Ca2+-ATPase
by 1,2-Cyclohexanedione Causes Inhibition of Formation of the Phosphoenzyme
Intermediate from
Inorganic Phosphate. J. Biol. Chem. Vol.272 (34), 21142-21150,
1997
12. Keisuke Kimura, Hiroshi
Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic
Reticulum Ca2+-ATPase. Modification with 1,2-Cyclohexanedione.
J. Biol. Chem. Vol.271 (46), 28933-28941, 1996
13. Tohru Kanazawa, Hiroshi
Suzuki, Takashi Daiho, and Kazuo Yamasaki.
Fluorometric Study on Conformational Changes in the Catalytic Cycle of
Sarcoplasmic Reticulum Ca2+-ATPase.
Bioscience Reports
Vol.15 (5), 317-326, 1995
14. Takashi Daiho and Tohru
Kanazawa.
Reduction of Disulfide Bonds in Sarcoplasmic Reticulum Ca2+-ATPase
by Dithiothreitol Causes Inhibition of Phosphoenzyme Isomerization in Catalytic
Cycle : This Reduction
Requires Binding of Both Purine Nucleotide and Ca2+to Enzyme.
J.
Biol. Chem., Vol.269, 11060-11064 , 1994
15. Kazuo Yamasaki, Takashi
Daiho, and Tohru Kanazawa.
3'-O-(5-Fluoro-2,4-dinitrophenyl)-ATP Exclusively Labels Lys-492
at the Active Site of the Sarcoplasmic Reticulum Ca2+-ATPase.
J. Biol. Chem., Vol.269, 4129-4134, 1994
16. Kazuo Yamasaki, Takashi
Daiho, and Tohru Kanazawa.
Labeling of Lysine 492 with Pyridoxal 5'-Phosphate in the Sarcoplasmic
Reticulum Ca2+-ATPase : Lysine 492 Residue is Located Outside
the Fluorescein
5-Isothiocyanate-Binding Region in or near the ATP Binding Site. J.
Biol. Chem., Vol.268, 20930-20936, 1993
17. Takashi Daiho, Tatsuya
Kubota, and Tohru Kanazawa.
Stoichiometry of Tight Binding of Magnesium and Fluoride to Phosphorylation
and High-Affinity Binding of ATP, Vanadate, and Calcium in the Sarcoplasmic
Reticulum
Ca2+-ATPase.
Biochemistry, Vol.32, 10021-10026,
1993
18. Tatsuya Kubota, Takashi
Daiho, and Tohru Kanazawa.
Quasi-irreversible Inactivation of the Sarcoplasmic Reticulum Ca2+-ATPase
by Simultaneous Tight Binding of Magnesium and Fluoride to the Catalytic
Site.
Biochim. Biophys. Acta, Vol.1163, 131-143, 1993
19. Yamamoto, T., Daiho,
T., and Takisawa, H.
Reconstitution of Calcium Transport from Monomeric ATPase of Sarcoplasmic
Reticulum.
Perspectives of Biological Energy Transduction,(Mukohata, Y., Morales,
M.F., and Fleischer, S.) 147-154, 1987
20. Daiho, T., Takisawa,
H., and Yamamoto, T.
Inhibition of hydrolysis of phosphorylated Ca2+,Mg2+-ATPase
of the sarcoplasmic reticulum by Ca2+ inside and outside the
vesicles.
J. Biochem.(Tokyo) Vol.97(2), 643-653, 1985
ŽR@è@@˜a@¶
1. Kazuo Yamasaki,
Takashi Daiho, and Hiroshi Suzuki.
Remarkable
Stability of Solubilized and Delipidated Sarcoplasimc Reticulum Ca2+-ATPase
with Tightly Bound Fluoride and Magnesium against Detergent-induced
Denaturation.
J.
Biol. Chem. in press, 2002
2. Stefania Danko,
Kazuo Yamasaki, Takashi Daiho, Hiroshi Suzuki, and Chikashi Toyoshima.
Organization
of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase
in E1P and E1ATP states: a limited proteolysis study.
FEBS Letters,
Vol.505, 129-135, 2001
3. Takashi Daiho,
Kazuo Yamasaki, Tomoyuki Saino, Mika Kamidochi, Katsuhiko Satoh, Hajime
Iizuka, and Hiroshi Suzuki.
Mutations of Either or both of Cys876 and Cys888 of Sarcoplasmic Reticulum
Ca2+-ATPase Result in a Complete Loss of Ca2+ Transport
Activity without a Loss of
Ca2+-ATPase activity, J. Biol. Chem. Vol.276(35),
32771-32778, 2001
4. Stefania Danko,
Takashi Daiho, Kazuo Yamasaki, Mika Kamidochi, Hiroshi Suzuki, and Chikashi
Toyoshima.
ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase
has a compact conformation resistant to proteinase K, V8 protease and trypsin.
FEBS Letters, Vol. 498(2-3), 277-282, 2001
5. Hiroshi Suzuki,
Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Only half of the Ca2+-ATPase molecules present in sarcoplasmic
reticulum vesicles can be phosphorylated with ATP or Inorganic phosphate.
Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier,
North Holland, 381-388, 2000
6. Takashi Daiho,
Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or specific substitutions of a few residents in the NH2-terminal
Ala3-Thr9 region of sarcoprasmic reticulum Ca2+-ATPase cause
inactivation and rapid degradation
of the enzyme expressed in COS-1 cells. Na/K-ATPase and Related ATPases.(K.Taniguchi
and S.Kaya Eds.)Elsevier, North Holland, 293-296, 2000
7. Kazuo Yamasaki,
Takashi Daiho, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations of arginine-198 in sarcoplasmic reticulum Ca2+ATPase
cause inhibition of hydrolysis of the phosphoenzyme intermediate formed
from inorganic phosphate.
Na/K-ATPase and Related ATPases.(K.Taniguchi and S.Kaya Eds.)Elsevier,
North Holland, 297-300, 2000
8. Takashi Daiho,
Kazuo Yamasaki, Hiroshi Suzuki, Tomoyuki Saino, and Tohru Kanazawa.
Deletions or Specific Substitutions of a Few Residues in the NH2-terminal
Region (Ala3-Thr9) of Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inactivation and Rapid
Degradation of the Enzyme Expressed in COS-1 Cells. J. Biol. Chem.
Vol.274
(34), 23910-23915, 1999
9. Takashi Daiho,
Hiroshi Suzuki, Kazuo Yamasaki, Tomoyuki Saino, and Tohru Kanazawa.
Mutations of Arg198 in Sarcoplasmic Reticulum Ca2+-ATPase Cause
Inhibition of Hydrolysis of the Phosphoenzyme Intermediate Formed from
Inorganic Phosphate.
FEBS Letters Vol. 444 (1), 54-58, 1999
10. Kazuo Yamasaki, Takashi
Daiho, Tomoyuki Saino, and Tohru Kanazawa.
Modification of Histidine 5 in Sarcoplasmic Reticulum Ca2+-ATPase
by Dietyl Pyrocarbonate Causes Strong Inhibition of Formation of Phosphoenzyme
Intermediate from
Inorganic Phosphate.
J. Biol. Chem. Vol.272 (49), 30627-30636,
1997
11. Keisuke Kimura, Hiroshi
Suzuki, Takashi Daiho, Kazuo Yamasaki, and Tohru Kanazawa.
Identification of Arginyl Residues Located at the ATP Binding Site of Sarcoplasmic
Reticulum Ca2+-ATPase. Modification with 1,2-Cyclohexanedione.
J. Biol. Chem. Vol.271 (46), 28933-28941, 1996
‰Á@“¡@@‘@•c
1. Tomoko Tazawa,
Sanae Kato, Tsuyoshi Kato, and Kunihiko Konnno.
Role of neck region in the thermal aggregation of myosin. J.Agric.Food.Chem.
Vol.50, 196-202, 2002
2. Kunihiko Konno,
Takeshi Yamamoto, Masayuki Takahashi, and Sanae Kato.
Early structural changes in myosin rod upon heating of carp myofibrils.
J.Agric.Food.Chem.
Vol.48, 4905-4909, 2000
3. Sanae Kato and
Isao Yumoto.
Detection of the Na+-translocating NADH-quinone reductase in
marine bacteria using a PCR technique. Canadian Journal of Microbiology,
Vol.46, 325-332, 2000
4. Sanae Kato and
Kunihiko Konno. Filament Formation of Carboxyl- and Amino-Group-Modified
Carp Myosin Rod.
Fisheries Science, Vol.66, 124-129,2000
5. Sanae Kato, Hiroaki
Koseki, and Kunihiko Konno. Oligomerization of carp myosin which retains
its ATPase activity. Fisheries Science, Vol.62(6), 985-989,1996
6. Sanae Kato and
Kunihiko Konno.
Substructure of tilapia myosin rod and its filament
forming ability.
Fisheries Science, Vol.62(3), 439-443,1996
7. Sanae Kato and
Kunihiko Konno.
Isolation of carp myosin rod and its structural stability.
“ú–{…ŽYŠw‰ïŽA59ŠªA539-544A1993
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