Polymorphic hemoglobin from a midge larva ( Tokunagayusurika akamusi) can be divided into two different types
The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VII, IX) on a DEAE-cellulose column. However, we found that these components can be divid...
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Published in | Biochimica et biophysica acta Vol. 1157; no. 3; pp. 185 - 191 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
11.06.1993
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Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 1878-2434 |
DOI | 10.1016/0304-4165(93)90063-E |
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Abstract | The hemoglobin from the 4th-instar larva of
Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VII, IX) on a DEAE-cellulose column. However, we found that these components can be divided into two groups on the basis of their spectroscopic properties, one being named as the normal type (N-type) and the other being referred to as low type (L-type). Since the major difference between them seemed to be the presence or absence of the distal (E7) histidine residue, which plays an important role in the stability properties of the bound dioxygen, the complete amino acid sequence was then determined for each typical component, namely, VII (N-type) and V(L-type): the former hemoglobin contained the usual distal histidine residue at position 64, whereas the latter one replaced it by isoleucine at position 66. The homology test for 40 N-terminal amino acid residues of all components also demonstrates that
T. akamusi hemoglobin is composed of two different clusters showing a very early separation in the phylogenetic tree. |
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AbstractList | The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VIII, IX) on a DEAE-cellulose column. However, we have found that these components can be divided into two groups on the basis of their spectroscopic properties, one being named as the normal type (N-type) and the other being referred to as the low type (L-type). Since the major difference between them seemed to be the presence or absence of the distal (E7) histidine residue, which plays an important role in the stability properties of the bound dioxygen, the complete amino acid sequence was then determined for each typical component, namely, VII (N-type) and V (L-type): the former hemoglobin contained the usual distal histidine residue at position 64, whereas the latter one replaced it by isoleucine at position 66. The homology test for 40 N-terminal amino acid residues of all components also demonstrates that T. akamusi hemoglobin is composed of two different clusters showing a very early separation in the phylogenetic tree. The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VII, IX) on a DEAE-cellulose column. However, we found that these components can be divided into two groups on the basis of their spectroscopic properties, one being named as the normal type (N-type) and the other being referred to as low type (L-type). Since the major difference between them seemed to be the presence or absence of the distal (E7) histidine residue, which plays an important role in the stability properties of the bound dioxygen, the complete amino acid sequence was then determined for each typical component, namely, VII (N-type) and V(L-type): the former hemoglobin contained the usual distal histidine residue at position 64, whereas the latter one replaced it by isoleucine at position 66. The homology test for 40 N-terminal amino acid residues of all components also demonstrates that T. akamusi hemoglobin is composed of two different clusters showing a very early separation in the phylogenetic tree. The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VIII, IX) on a DEAE-cellulose column. However, we have found that these components can be divided into two groups on the basis of their spectroscopic properties, one being named as the normal type (N-type) and the other being referred to as the low type (L-type). Since the major difference between them seemed to be the presence or absence of the distal (E7) histidine residue, which plays an important role in the stability properties of the bound dioxygen, the complete amino acid sequence was then determined for each typical component, namely, VII (N-type) and V (L-type): the former hemoglobin contained the usual distal histidine residue at position 64, whereas the latter one replaced it by isoleucine at position 66. The homology test for 40 N-terminal amino acid residues of all components also demonstrates that T. akamusi hemoglobin is composed of two different clusters showing a very early separation in the phylogenetic tree.The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable components (IA, IB, II, III, IV, V, VIA, VIB, VII, VIII, IX) on a DEAE-cellulose column. However, we have found that these components can be divided into two groups on the basis of their spectroscopic properties, one being named as the normal type (N-type) and the other being referred to as the low type (L-type). Since the major difference between them seemed to be the presence or absence of the distal (E7) histidine residue, which plays an important role in the stability properties of the bound dioxygen, the complete amino acid sequence was then determined for each typical component, namely, VII (N-type) and V (L-type): the former hemoglobin contained the usual distal histidine residue at position 64, whereas the latter one replaced it by isoleucine at position 66. The homology test for 40 N-terminal amino acid residues of all components also demonstrates that T. akamusi hemoglobin is composed of two different clusters showing a very early separation in the phylogenetic tree. |
Author | Fukuda, Mitsunori Shikama, Keiji Takagi, Takashi |
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Cites_doi | 10.1016/0022-2836(89)90012-0 10.1016/0378-1119(88)90344-7 10.1016/0022-2836(82)90515-0 10.3891/acta.chem.scand.02-0264 10.1515/bchm2.1979.360.1.115 10.1515/bchm2.1981.362.1.539 10.1111/j.1399-3011.1973.tb03452.x 10.1515/bchm3.1989.370.1.533 10.1111/j.1432-1033.1971.tb01285.x 10.1016/0022-2836(84)90277-8 10.1016/0003-2697(77)90381-5 10.1515/bchm2.1965.340.1-2.88 10.1515/bchm2.1981.362.1.261 10.1515/bchm2.1981.362.1.59 10.1515/bchm2.1968.349.1.197 10.1016/0005-2795(81)90225-7 10.7601/mez.29.93 10.1016/0003-9861(59)90090-6 10.1515/bchm2.1979.360.1.89 10.1515/bchm2.1980.361.1.933 10.1016/0022-2836(79)90332-2 10.1515/bchm2.1979.360.1.99 |
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Snippet | The hemoglobin from the 4th-instar larva of
Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable... The hemoglobin from the 4th-instar larva of Tokunagayusurika akamusi, a common midge found in eutrophic lakes in Japan, was composed of as many as 11 separable... |
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SubjectTerms | Amino Acid Sequence amino acid sequences Animals biochemical polymorphism Chemical Fractionation chemistry Diptera Diptera - chemistry Distal · His Hemoglobin Hemoglobins Hemoglobins - chemistry Hemoglobins - isolation & purification Histidine isolation & purification Isoleucine Larva Larva - chemistry larvae Midge ( Tokunagayusurika) Molecular Sequence Data Phylogeny Polymorphism Sequence Alignment tokunagayusurika akamusi |
Title | Polymorphic hemoglobin from a midge larva ( Tokunagayusurika akamusi) can be divided into two different types |
URI | https://dx.doi.org/10.1016/0304-4165(93)90063-E https://www.ncbi.nlm.nih.gov/pubmed/8507654 https://www.proquest.com/docview/48448356 https://www.proquest.com/docview/75787372 |
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