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  • 1
    ISSN: 0032-8332
    Keywords: Sulawesi macaque ; Celebes macaque ; Macaque ; Macaca ; Hemoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The monkeys on the island of Sulawesi (Celebes), Indonesia, comprise seven species ofMacaca, that isM. maura, M. tonkeana, M. hecki, M. nigrescens, M. nigra, M. ochreata, andM. brunnescens. Hemoglobins from 248 individuals of these seven species were analyzed by isoelectric focusing electrophoresis (IEFE) and by starch gel electrophoresis in the presence of urea (USGE). Eighteen phenotypes consisting of eight molecular types were identified by IEFE analysis. The speciestonkeana inhabiting the central part of the island revealed 11 phenotypes, while peripheral species such asnigrescens andbrunnescens carried only 3 and 2 phenotypes, respectively. On USGE, three α chains and three β chains were identified and named α1, α2, and α6, and β1, β3, and β5, respectively. The α1 chain has the same mobility as the α chains of other macaques, while the α2 chain is less positively charged than α1, and α6 is the least positive among these α chains. The α2 chain is widely distributed in the Sulawesi macaques as the major component. Four species,ochreata, tonkeana, maura, andnigrescens, carried the α1 and α6 chains as minor components. The electrophoretic mobility of β1 was the same as that of other macaques, while β3 and β5 were more positively charged and less positively charged than β1, respectively. All of the Sulawesi species had β3 in high or low gene frequencies and inmaura, tonkeana, andbrunnescens, this type was most abundant. β5 chain existed in the species of the northern peninsula, as the major type. The subordinate type was β3 innigra andnigrescens and β1 inhecki. On the other hand, β1 was most frequently observed inochreata.
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  • 2
    ISSN: 0032-8332
    Keywords: Hemoglobin ; Variant hemoglobin ; Macaca fuscata ; Hb Izu (Macaca) ; Primates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A hemoglobin variant was discovered in Japanese monkeys (Macaca fuscata) of the Wakinosawa A-1 troop of the Shimokita peninsula, the northernmost limit of this species' habitat. The variant was characterized by slow migration on starch gel electrophoresis due to its polymerizing nature. Structural analysis revealed that Gly at the 83rd amino acid residue of theβ chain was substituted by Cys, and the variant was identified as Hb Izu (Macaca). The gene frequency of the variant was extremely high, at 85.7%, and much higher than the 21.3% obtained for the troops of the Izu peninsula. The genotypic frequencies in the troops of both the Izu and Shimokita peninsulas agreed with expectations as calculated from the Hardy-Weinberg equilibrium.
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  • 3
    ISSN: 0032-8332
    Keywords: Hemoglobin ; Variant hemoglobin ; Macaca fascicularis ; Hb Bali (Macaca) ; Primates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A variant hemoglobin due to structural change in the β chain was found in the central part of Bali island, Indonesia, during field studies on the genetic variation of the Indonesian crabeating monkey (Macaca fascicularis), and was named Hb Bali (Macaca). Structural analysis yielded the following results. (1) The amino acid sequence of the normal β chain of the crab-eating monkey coincided with that of the Japanese monkey (M. fuscata) and the pig-tailed monkey (M. nemestrina). (2) Asn at the 80th position from the amino terminal of the β chain was substituted by Lys in Hb Bali. This substitution appeared to have little harmful effect on the carrier, since the hematological characteristics of the heterozygous carriers were not different from those of normal individuals.
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  • 4
    ISSN: 0032-8332
    Keywords: Sulawesi macaque ; Celebes macaque ; Macaca ; Primary structure ; Hemoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Seven β chains were identified as the typical molecular types carried by the seven species of Sulawesi macaques based on isoelectric focusing and urea starch gel electrophoresis. These β chains include the β3 chains ofmaura, tonkeana, nigra, andbrunnescens, β1 chains ofhecki andochreata and β5 chain ofnigra. The results of chromatography on cation-exchange and reversed phase columns and the amino acid compositions of the tryptic peptides suggested substitutions at the 9th and 13th amino acids from the N-terminal. Sequence analyses of these seven β chains from the N-terminal to the 18th amino acid and those of purified tryptic peptides from βT3 to βT15 by Edman degradation revealed the following facts: (1) the amino acid sequences of the β3 chains carried by the four species coincided with each other and as did those of the β1 chains of the two named species; and (2) the 9th and 13th amino acids were Lys and Thr in β3, Asn and Asn in β1, and Asp and Thr in the β5 chain, respectively. These three β chains are related with each other by at least two-base changes. The evolution of the β chains of the Sulawesi macaques was inferred to be as follows. (1) The β3 chain might have been dominant β chain in the past among Sulawesi macaques, since peripheral species separately carried this chain; (2) the β1 and β5 chains might have derived from a “missing link” because of more than two-base substitutions between β3 and β1 and between β3 and β5; (3) eight other macaque species, including the lion-tailed macaque (M. silenus), bear Asn and Thr at these two positions, while the Barbary macaque (M. sylvanus) has Thr and Thr; and (4) thus, if the parsimonious rule is followed, the type with Asn-Thr is the most plausible “missing link,” since only the Asn-Thr type can combine these five β chains by minimum one-base change. Two genetic events are postulated in the evolutionary process of the Sulawesi β chains: the first Lys-Thr type (β3) was distributed over the whole island, and next Asn-Thr, the common type in other macaques, produced Asn-Asn (β1) and Asp-Thr (β5).
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