Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Keiji Shikama"'
Publikováno v:
Applied Magnetic Resonance. 31:527-541
The coordination of small molecules and ions at the sixth position of ferric myoglobins (Mb) from the heart muscle of two species of shark,Lamna ditropis (LD) andPrionace glauca (PG), was studied in frozen solution by electron paramagnetic resonance
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76208985a55cc3063d7811ee71269aaf
https://doi.org/10.1007/bf03166600
https://doi.org/10.1007/bf03166600
Autor:
Keiji Shikama
Publikováno v:
Progress in Biophysics and Molecular Biology. 91:83-162
The iron(II)-dioxygen bond in myoglobin and hemoglobin is a subject of wide interest. Studies range from examinations of physical-chemical properties dependent on its electronic structure, to investigations of the stability as a function of oxygen su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e04f806fa1f2212a19edafe6ff56210
https://doi.org/10.1016/j.pbiomolbio.2005.04.001
https://doi.org/10.1016/j.pbiomolbio.2005.04.001
Autor:
Ariki Matsuoka, Keiji Shikama
Publikováno v:
Critical Reviews in Biochemistry and Molecular Biology. 39:217-259
Based on the literature and our own results, this review summarizes the most recent state of nonvertebrate myoglobin (Mb) and hemoglobin (Hb) research, not as a general survey of the subject but as a case study. For this purpose, we have selected her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be6d0ec3bbdd1ab78ad25fdf390fa512
https://doi.org/10.1080/10409230490514008
https://doi.org/10.1080/10409230490514008
Autor:
Ariki Matsuoka, Keiji Shikama
Publikováno v:
European Journal of Biochemistry. 270:4041-4051
This review summarizes the most recent state of haemoglobin (Hb) research based on the literature and our own results. In particular, an attempt is made to form a unified picture for haemoglobin function by reconciling the cooperative oxygen binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15eed7ea1c48e0588f0399e987977fca
https://doi.org/10.1046/j.1432-1033.2003.03791.x
https://doi.org/10.1046/j.1432-1033.2003.03791.x
Autor:
Keiji Shikama, Gen Kobayashi, Hitoshi Ohmachi, Takehiko Ochiai, Takashi Nakamura, Ariki Matsuoka
Publikováno v:
Journal of Biological Chemistry. 277:42540-42548
Flavohemoglobin was isolated directly from the yeast Candida norvegensis and studied on its structural, spectral, and stability properties. In Candidaflavohemoglobin, the 155 N-terminal residues make a heme-containing domain, while the remaining 234
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::636aa87365d5aabdaa2e8edbfc246399
https://doi.org/10.1074/jbc.m206529200
https://doi.org/10.1074/jbc.m206529200
Publikováno v:
European Journal of Biochemistry. 269:202-211
When the α and β chains were separated from human oxyhemoglobin (HbO2), each individual chain was oxidized easily to the ferric form, their rates being almost the same with a very strong acid-catalysis. In the HbO2 tetramer, on the other hand, both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b12d9bd94bd4cf8d9a2fff8199a9b98
https://doi.org/10.1046/j.0014-2956.2002.02635.x
https://doi.org/10.1046/j.0014-2956.2002.02635.x
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385:89-100
One of the components of hemoglobin from the larval hemolyph of Tokunagayusurika akamusi possesses naturally occurring substitution at the E7 helical position (Leu E7) [M. Fukuda, T. Takagi, K. Shikama, Biochim. Biophys. Acta 1157 (1993) 185–191].
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b22296859a4e038cc385a73c98e928b
https://doi.org/10.1016/s0167-4838(98)00051-x
https://doi.org/10.1016/s0167-4838(98)00051-x
Publikováno v:
Journal of Biological Chemistry. 273:8607-8615
Human oxyhemoglobin showed a biphasic autoxidation curve containing two rate constants, i.e. kf for the fast autoxidation due to the α chains, and ks for the slow autoxidation of the β chains, respectively. Consequently, the autoxidation of the HbO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68050e3d230e2a6efad08d551b14e68b
https://doi.org/10.1074/jbc.273.15.8607
https://doi.org/10.1074/jbc.273.15.8607
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 115:483-492
With regard to the distal (E7) residue, gastropod sea mollusc contains both types of myoglobin, one with and the other lacking the distal histidine. We have isolated a myoglobin from the radular muscle of Cerithidea rhizophorarum, a small whelk found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f62aa7c52b4dbfd73e793603a8c2e1f
https://doi.org/10.1016/s0305-0491(96)00162-9
https://doi.org/10.1016/s0305-0491(96)00162-9
Publikováno v:
European Journal of Protistology. 32:73-78
Summary A myoglobin-like protein from Tetrahymena pyriformis is composed of 121 amino acid residues with a molecular mass of 14,343 daltons including the heme moiety. This is much smaller than sperm whale myoglobin, i. e. by 32 residues and shows no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d31faa860b52a76a5c2533807550c00
https://doi.org/10.1016/s0932-4739(96)80080-0
https://doi.org/10.1016/s0932-4739(96)80080-0