Studies on the subunits of myosin from muscle layer of Ascaris lumbricoides suum

Nakamura, Takeshi; Yanagisawa, Toshio; Yamaguchi, Masahiro

doi:10.1016/0005-2795(75)90037-9

Cited by 8 publications

(1 citation statement)

References 25 publications

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“…Invertebrate isoforms. One of the most primitive muscle myosins so far examined in detail is that from the Nematode Ascaris lumbricoides (Ko et al, 1979) which contains two myosin light chains of Mr 16000 and 18000 (Nakamura et al, 1975), the larger of which can be liberated with DTNB and corresponds to the MLC2 or regulatory light chain. The second light chain shows an electrophoretic mobility comparable with that of the vertebrate MLC3F and of smooth muscle/non-muscle isoforms.…”

Section: Myosin Alkali Light Chains In Other Animals; Evolutionary Asmentioning

confidence: 99%

The myosin alkali light chain proteins and their genes

Barton¹,

Buckingham²

1985

Biochemical Journal

171

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Section: Myosin Alkali Light Chains In Other Animals; Evolutionary Asmentioning

confidence: 99%

The myosin alkali light chain proteins and their genes

Barton¹,

Buckingham²

1985

Biochemical Journal

171

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Polymorphism of contractile proteins

Gros

Buckingham

1987

Biopolymers

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SynopsisContractile proteins are present as multiple isoforms encoded by multigene families. The numbers of known isoforms of the myosins, actins, tropomyasins, and troponins are summarized, and the mechanisms by which this diversity has been generated are discussed. Two major strategies can be distinguished, one that depends on gene duplication events leading to the appearance of complete new structural genes, and a second that involves differential splicing of exons within a single complex gene. This latter mechanism is particularly prevalent among the contractile protein families. The developmental regulation of isoform expression is reviewed in the context of these strategies. The biological significance of contractile protein polymorphism is d i s c u s s e d .

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Detection and localization of actin inToxoplasma gondii

et al. 1988

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The immunological cross-reactivity of the protein from whole-cell extracts of Toxoplasma gondii with antisera against actins from chicken-gizzard smooth muscle and from Ascaris body-wall muscle was demonstrated by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis (SDS-PAGE) and immunofluorescence studies. A protein of about 42 kDa, with the same mobility as that of rabbit smooth-muscle actin in SDS-PAGE showed cross-reactivity with anti-actin antisera on the electroblotted nitrocellulose sheet. Indirect fluorescent antibody staining of the parasites clearly showed that actin localized strongly in the anterior third of the organism in both extra- and intrahost cellular stages. From both a biochemical as well as structural point of view, the results obtained in the present experiments might explain the locomotive features of the parasite such as twirling and sliding, with most of the activity at the anterior end.

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Studies on the subunits of myosin from muscle layer of Ascaris lumbricoides suum

Cited by 8 publications

References 25 publications

The myosin alkali light chain proteins and their genes

The myosin alkali light chain proteins and their genes

Polymorphism of contractile proteins

Detection and localization of actin inToxoplasma gondii

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