Tropomyosin, myosin and actin from the blowfly, Phormia regina

Kominz, David R.; Maruyama, Kosçak; Levenbook, L.; Lewis, Marc S.

doi:10.1016/0006-3002(62)90343-8

Cited by 46 publications

(12 citation statements)

References 25 publications

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“…Amino acid composition of the paramyosin-free insect myosins (Table 1) is similar to but not identical with that previously reported for rabbit (Lowey & Cohen, 1962) and Phormia (Kominz et al, 1962) myosins. Insect myosin has more glutamic acid and less lysine than myosin from rabbit muscle.…”

Section: Resultssupporting

confidence: 83%

Purification of insect myosin and α-actinin

Hammond¹,

Goll²

1975

Biochemical Journal

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Section: Resultssupporting

confidence: 83%

Purification of insect myosin and α-actinin

Hammond¹,

Goll²

1975

Biochemical Journal

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“…But it must be borne in mind that this arrangement might not apply outside vertebrate muscle. In insect flight muscle, which contains tropomyosin B (Kominz, Maruyama, Levenbock & Lewis 1962), the thin filaments branch into only two subfila ments as they pass into the Z-line (Auber & Couteaux 1963). It is interesting that no axial periodicity has been described in insect flight muscle, as Hodge ( 1956) also pointed out.…”

Section: (C)mentioning

confidence: 99%

The structure of actin filaments and the origin of the axial periodicity in the I -substance of vertebrate striated muscle

Hanson

Lowy

1964

Proc. R. Soc. Lond. B.

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Certain advances due mainly to H. E. Huxley (see Huxley 1961, 1963) have made it possible to use the electron microscope to study the detailed structure of the filaments in the contractile apparatus. The results of our work on actin filaments have already been published (Hanson & Lowy 1962, 1963). We shall now examine some of the consequences of these findings, including certain unsolved problems which they raise. Actin in the polymerized form ( F -actin) has been prepared from rabbit skeletal muscle by the usual methods and examined in negatively stained preparations in the electron microscope (Hanson & Lowy 1963). It has been found that solutions of F -actin are, in fact, suspensions of filaments. These consist of globular subunits arranged in a characteristic helical manner (figure 15).

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“…Glycerinated fibres of fibrillar muscle require Ca2+ for activity, as do fibres of non-fibrillar muscle, but they can be further activated by a small amount of stretching (Ruegg & Tregear, 1966;Chaplain, 1967). Studies on proteins isolated from fibrillar muscle (Kominz, et al, 1962;Maruyama, 1965) have shown that the major proteins of the myofibril are similar to those of vertebrate striated muscle. However, there have been reports that myofibrils and actomyosin from fibrillar muscle are activated less by Ca2+ than are the same preparations from non-fibrillar muscle (vom Brocke, 1966;Maruyama et al, 1968).…”

mentioning

confidence: 99%

The contractile and regulatory proteins of insect flight muscle

Bullard

Da̧browska

Winkelman

1973

Biochemical Journal

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1. Myosin, actin and the regulatory proteins were prepared from insect flight muscle. 2. The light subunit composition of the myosin differed from that of vertebrate muscle myosin. The ionic strength and pH dependence of the myosin adenosine triphosphatase (ATPase) were measured. 3. Actin was associated with a protein of subunit molecular weight 55000 and was purified by gel filtration. Impure actin had protein bound at a periodicity of about 40nm. 4. Regulatory protein extracts had tropomyosin and troponin components of subunit molecular weight 18000, 27000 and 30000. Crude extracts of regulatory proteins inhibited the ATPase activity of desensitized or synthetic actomyosin; this inhibition was relatively insensitive to high Ca(2+) concentrations. Purified insect regulatory protein produced as much sensitivity to Ca(2+) as did the rabbit troponin-tropomyosin complex. 5. Synthetic actomyosins were made from rabbit and insect proteins. Actomyosins containing insect myosin had a low ATPase activity that was activated by tropomyosin. The Ca(2+) sensitivity of actomyosins containing insect myosin or actin, with added troponin-tropomyosin complex from rabbit, was comparable with that of rabbit actomyosin.

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Tropomyosin, myosin and actin from the blowfly, Phormia regina

Cited by 46 publications

References 25 publications

Purification of insect myosin and α-actinin

Purification of insect myosin and α-actinin

The structure of actin filaments and the origin of the axial periodicity in the I -substance of vertebrate striated muscle

The contractile and regulatory proteins of insect flight muscle

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