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  2. 生命科學院
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請用此 Handle URI 來引用此文件: http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75933
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DC 欄位值語言
dc.contributor.authorPu-Sen Bien
dc.contributor.author畢璞仙zh_TW
dc.date.accessioned2021-07-01T08:16:33Z-
dc.date.available2021-07-01T08:16:33Z-
dc.date.issued1992
dc.identifier.citationArmstrong, D.L. (1989)
Calcium channel regulation by calcineurin, a Ca2+—activated 59
phosphatase in mammalian brain
TINS 12:117—122
Bachs, O., Lanini, L., Sarratos, J., Coll, M.J., Bastos, R.,
Aligu?, R., Rius, E. and Carafoli, E. (1990)
Calmodulin-binding proteins in the nuclei of quiescent and
proliferatively activated rat liver cells
J. Bid. Chem. 265:18595—18600
Baudier, J., Bronner, C., Kligman, D. and Cole, R.D. (1989)
Protein kinase C substrates from bovine brain
J. Biol. Chem. 264:1824—1828
Berridge, M.J. (1987)
Inositol trisphosphate and diacylglycerol: two interacting second
messengers
Ann. Rev. Biochem., 56:159—193
Berridge, M.J. and Galione, A. (1988)
Cytosolic calcium oscillators
FASEB J., 2:3074—3082
Berridge, N.J. and Irvine, R.F. (1989)
Inositol phosphates and cell signaling
Nature, 341:197—205
Berridge, M.J. and Irvine, R.F. (1984)
Inositol trisphosphate, a novel second messenger in cellular signal
transduction
Nature, 312:315—321
Billingsley, M.L., Pennypacker, K.R., Hoover, C.G., Brigati, D.J.
and Kincaid, R.L. (1985)
A rapid and sensitive method for detection and quantification of
calcineurin and calmodulin-binding proteins using biotinylated
calmodulin
P.N.A.S. 82:7585—7589
Boyle, W.J., Smeal, T., Defize, L.H.K., Angel, P., Woodgett, J.R.,
Karin, M. and Hunter, T. (1991)
Activation of protein kinase C decreases phosphorylation of c—Jun
at sites that negatively regulate its DNA-binding activity
Cell 64:573—584
Calcium and Calcium—Binding Proteins, by Anthony R. Means (1987) Methods in Enzymology, Vol. 139, Cellular regulators, Part A,
Chapman, E.R., Au, D., Alexander, K.A., Nicolson, T.A. and Storm,
D.R. (1991)
Characterization of the calmodulin binding domain of neuromodulin
J. Biol. Chem. 266:207—213
Claudia A.R. da Silva and Reinach, F.C. (1991)
Calcium binding induces conformational changes in muscle regulatory
proteins, TIBS 16:53—57
Croall, D.E. and Demartino, G.N. (1991) Calcium—activated neutral protease (calpain) system: structure, function, and regulation
Physiol. Rev. 71:813—847
Fournierand, S. and Trifar?, J.M. (1988)
A similar calmodulin—binding protein expressed in chromaff in,
synaptic, and neurohypophyseal secretory vesicles
J. Neurochem., 50:27—37
Geiser, J.R.,, van Tuinen, D., Brockerhoff, S.E., Neff, M.M. and
Davis, T.N. (1991)
Can calmodulin function without binding calcium
Cell 65:949—959
Hashimoto, Y., Perrino, B.A. and Soderling, T.R. (1990)
Identification of an autoinhibitory domain in calcineurin
J. Biol. Chem. 265:1924—1927
Heizman, C.W. and Hunziker, W. (1991)
Intracellular calcium—binding proteins: More sights than insights
TIBS 16:98—103
Hemmings, JR., H.C., Nairn, A.C., McGuinness, T.L., Hnganir, R.L.
and Greengard, P. (1989)
Role of protein phosphorylation in neuronal signal transduction
FASEB J. 3:1583—1592
Huang, K.P. (1989)
The mechanism of protein kinase C activation
TINS 12:425—432
Ichimura, T., Sugano, H., Kuwano, R., Sunaya, T., Okuyama, T. and
Isobe, T.
Widespread distribution of the 14-3-3 protein in vertebrate brains and bovine tissues: correlation with the distributions of calcium— dependent protein kinases
J. Neurochem. 56:1449-1451
Jarrett, H.W. and Madhavan, R. (1991)
Calmodulin—binding proteins also have a calmodulin-like binding
site within their structure
J. Biol. Chem. 266:362—371
Kennedy, M.B. (1989) a
Regulation of neuronal function by calcium
TINS 12:417—420
Kennedy, M.B. (1989)b
Regulation of synaptic transmission in the central nervous system:
long-term potentiation
Cell 59:777—787
Klee, C.B., Crouch, T.H. and Richman, P.G. (1980)
Calmodulin, Ann. Rev. Biochem. 49:489—515
Lefkowitz, R.J., Hausdorff, W.P. and Caron, M.G. (1990)
Role of phosphorylation in desensitization of the B-adrenoceptor
TiPS 11:190—194
Llin?s, R., McGuinness, T.L., Leonard, C.S., Sugimori, M. and
Greengard, P.
Intraterminal injection of synapsin I or calcium/calinodulin—
dependent protein kinase IIalters neurotransmitter release at the
squid giant synapse
P.N.A.S. 82:3035—3039
Lohse, M.J., Benovie, J.L., Caron, M.G. and Lefkowitz, R.J. (1990)
Multiple pathways of rapid B2-adrenergic receptor desensitization
J. Biol. Chem. 265:3202—3209
Maruyama, K., Mikawa, T. and Ebashi, S. (1984)
Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
J. Biochem., 95:511—519
Means, A.R., Tash, J.S. and Chafouleas, J.D. (1982)
Physiological implication of the presence, distribution, and
regulation of calmodulin in eukaryotic cells, Physiol. Rev. 62:1-
39
Melloni, E. and Pontremoli, S. (1989)
The calpains
TINS 12:438—444
Merril, C.R., Goldman, D. and Van Keuren, M.L. (1984)
Gel protein stains: silver stain
Methods in Enzymology, 104:441-447
Miller, S.G. and Kennedy, M.B. (1985)
Distinct forebrain and cerebellar isozymes of type II
Ca2/calmodu1in—dependent protein kinase associate differently with
the postsynaptic density fraction
J. Biol. Chem. 260:9039—9046
Milner, R.E., Ba]csh, S., Shemanko, C., Carpenter, M.R., Smillie, L., Vance, J.E., Opas, M. and Michalak, M.
Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum
J. Biol. Chem. 266:7155—7165
Najrn, A.C. and Greengard, P (1987)
Purification and characterization of Ca /Calmodu1in—dependent
protein kinase I from bovine brain, J. Biol. Chem. 262:7273—7281
O’Neil, K.T. and DeGrado, W.F. (1990)
How calmoduljn binds its targets: sequence independent recognition
of amphiphilic α—helices
TIBS 15:59—64
Paupardin—Tritsch, D., Hammond, C., Gerschenfeld, H.M., Nairn,
A.C. and Greengard, P. (1986)
C—GMP—dependent protein kinase enhances Ca2+ current increase in
snail neurons
Nature, 323:812—814
Persechini, A., Moncrief, N.D. and Kretsinger, R.H. (1989)
The EF-hand family of calcium modulated proteins, TINS 12:462-467
Principles of Neural Sciences, third edtion, Elsevier science
publishing
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Use of calmodulin-agarose ALD in the purification of calcium
dependent calmodulin kinase
Focus 13:63—65
Rasmussen, C.D. and Means, A.R. (1989)
Calmodulin, cell growth and gene expression
TINS 12:433—438
Rieker, J.P., Swanljung-Collins, H. and Collins, J.H. (1987)
Purification and characterization of a calmodulin—dependent myosin
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J. Biol. Chem., 262:15262—15268
Roach, P.J. (1990)
Control of glycogen synthase by hierarchal protein phosphorylation
FASEB J. 4:2961—2968
Salacinski, P.R.P., McLean, C., Sykes, J.E.C., Clement—Jones, V.V.
and Lowry, P.J. (1981)
Iodination of proteins, glycoproteins, and peptides using a solid- phase oxidizing agent, 1,3,4, 6-tetrachloro-3a, 6a-diphenyl
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Anal. Biochem., 117:136—146
Schulman, H. and Lou, L.L. (1989)
Multifunctional Ca2+/calmodulin—dependent protein kinase: domain
structure and regulation
TIBS 14:62—66
Sheorain, V.S., Khatra, B.S. and Soderling, T.R. (1982) Hormonal regulation of skeletal muscle glycogen synthase through
covalent phosphorylation
Federation Processing, 41:2618—2622
Siekevitz, P. (1991)
Possible role for calmodulin and the Ca2+ /calmodulin—dependent
protein kinase II in postsynaptic neurotransmission
P.N.A.S. 88:5374—5378
Sprang, S.R., Acharya, K.R., Goldsmith, E.J., Varvill, R.J.,
Madsen, N.B. and Johnson, L.N.
Structural changes in glycogen phosphorylase induced by
phosphorylation
Nature 336:215—221
Tsunoda, Y. (1991)
Oscillatory Ca2+ signaling and its cellular function
The New Biologist, 3:3—17
Vandrell, M., Aligu?, R., Bachs, O. and Serratosa, J. (1991)
Presence of calmodulin and calmodulin—binding proteins in the
nuclei of brain cells
J. Neurochem. 57:622—628
dc.identifier.urihttp://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75933-
dc.description.abstract細胞外界之訊息,如荷爾蒙、生長因數、神經傳導物質及電刺激等可藉second messengers 的傳遞引起細胞內的生化反應。已知的: second messengers有Ca2+、c-AMP 、 c-GMP、 Inositol trisphosphate 及Diacylglycerol 等。本論文在探討鈣離子的結合蛋白及嗜鈣蛋白( calmodulin ,一種鈣離子結合蛋白)的結合蛋白,試圖找尋與鈣離子有關,更下游的訊號傳遞者。本論文使用 5 %過氯酸( perchloric acid ,簡稱 PCA )萃取鯉魚大腦細胞質液,在蛋白質磷酸化分析中,發現 PCA 可溶蛋白可加強磷酸化反應之強度。在 SDS - PAGE 分析中,發現了 30kDa的鈣離子及嗜鈣蛋白結合蛋白。通過 HPLC C18 co1umn 後,發現此30kDa蛋白並非單純一種蛋白。以gel slicing method 製作此30kDa蛋白的抗體,發現其可專一地辨認一種 30kDa 蛋白。本論文也利用此抗體做 30kDa蛋白的免疫化學研究,發現在鯉魚大腦局部及腦下腺神經葉皆有此蛋白之分佈。有關此蛋白之確實性質尚待進一步研究。zh_TW
dc.description.abstractCells respond to a variety of external stimuli by fluctuation of concentrations of second messengers; such as calcium, cyclic adenosine monophosphate, cyclic guanosine monophosphate, inositol trisphosphate and diacylglycerol, which would then initiate a cascade of biochemical reactions within the cells. Calcium—binding proteins are believed to be the downstream regulators of calcium— initiated biochemical reactions. So far, more than twenty proteins have been identified with calcium-binding activity, but only a few of them have been demonstrated with definite physiological functions (protein kinase C, calcineurin, Ca2+/calmodulin—dependent protein kinases and calpain) . Therefore, we developed analytical methods for calcium-binding proteins and calmodulin-binding proteins in this thesis and tried to purify these binding proteins from carp brain. Using perchioric acid extraction, HPLC C18 column chromatography, Calmodulin—Sepharose affinity column chromatography, we have purified one calmodulin—binding protein of 30kDa and partially purified one calcium/calmodulin—binding protein also of 30kDa. Antiserum against this 30 k calmodulin— binding protein have been raised and used for Western blot analysis and immunocytochemistry study. Preliminary data suggest that the 30kDa calmodulin-binding protein is present only in neurohypophysis and certain areas of brain.en
dc.description.provenanceMade available in DSpace on 2021-07-01T08:16:33Z (GMT). No. of bitstreams: 0
Previous issue date: 1992
en
dc.description.tableofcontents英文摘要. . . . . . . . . . . . . . 1
摘要 . . . . . . . . . . . . . . . . . 2
緒言 . . . . . . . . . . . . . . . . .3
材料與方法. . . . . . . . . . . . . 8
結果. . . . . . . . . . . . . . . . . 23
討論. . . . . . . . . . . . . . . . . 27
圖表. . . . . . . . . . . . . . . . . 31
引用文獻. . . . . . . . . . . . . . 59
謝辭. . . . . . . . . . . . . . . . . 64
dc.language.isozh-TW
dc.title鯉魚大腦嗜鈣蛋白結合蛋白之純化與免疫化學研究zh_TW
dc.titleA 30kDa Ca2+ and Calmodulin Binding Protein in Carp Brain Purification & Immunochemical Studyen
dc.date.schoolyear80-2
dc.description.degree碩士
dc.relation.page67
dc.rights.note未授權
dc.contributor.author-dept生命科學院zh_TW
dc.contributor.author-dept生化科學研究所zh_TW
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