Isolation, purification and characterization of creatine kinase from bovine cardiac muscle

Herasymowych, O.Sonia; Mani, Rajam S.; Kay, Cyril M.

doi:10.1016/0005-2795(78)90473-7

Cited by 15 publications

(3 citation statements)

References 22 publications

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“…In this paragraph we shall therefore refer to Wine as the total ofstructural features within the middle of the H-zone, regardless of whether or not these structures are visible as a line in the electron microscope. It has been suggested that holding the myosin filaments in proper register might be the general function of the Wine (6,10,21). But what is the special function of each of the structural components of the Mline in different types of muscles?…”

Section: Function Of the Winementioning

confidence: 99%

“…Three structural elements have been identified: primary and secondary (Y-shaped) M-bridges and M-filaments (14,16,20,27,33,39) . Only vague notions exist on the function of this complex structure running across the sarcomere at the height ofthe bare zone of thick myosin filaments (6,10,21). To obtain more insight into this problem it would be of importance to learn more on the common features that make up the several structural components of the M-line region of the different types of muscle fibers.…”

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confidence: 99%

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Biochemical and ultrastructural aspects of Mr 165,000 M-protein in cross-striated chicken muscle.

Strehler¹,

Pelloni²,

Heizmann³

et al. 1980

The Journal of Cell Biology

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To better understand the relationship between the Mr 165,000 M-line protein (Mprotein) and H-zone structure in skeletal and in cardiac muscle, as well as the possible interaction of M-protein with another skeletal muscle M-line component, the homodimeric creatine kinase isoenzyme composed of two M subunits (MM-CK), we performed biochemical, immunological, and ultrastructural studies on myofibrils extracted by different procedures .In contrast to MM-CK, M-protein could not be completely removed from myofibrils by low ionic strength extraction . Fab-fragments of antibodies against M-protein could not release Mprotein quantitatively from either breast or heart myofibrils but remained bound to the myofibrillar structure, whereas monovalent antibodies against MM-CK cause the specific release of MM-CK and the concomitant disappearance of the M-line from chicken skeletal muscle myofibrils . When MM-CK was removed from skeletal myofibrils by low ionic strength extraction or, more specifically, by incubation with anti-MM-CK Fab, M-protein was still not released quantitatively upon treatment with anti-M-protein Fab as judged from immunofluorescence data . In the ultrastructural investigation of low ionic strength extracted muscle fibers, M-protein could be localized in two stripes on both sides of the former M-line, suggesting a reduced attachment to the residual H-zone structure, whereas the specific removal of MM-CK resulted in the same dense staining pattern for M-protein within the M-line as observed in untreated fibers . However, the binding of M-protein to the residual M-line structure seemed to be reduced, as a considerable amount of this protein could be identified in the supernate of sequentially incubated myofibrils . The results indicate a strong binding of M-protein within the H-zone structure of skeletal as well as heart myofibrils .

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Section: Function Of the Winementioning

confidence: 99%

mentioning

confidence: 99%

Biochemical and ultrastructural aspects of Mr 165,000 M-protein in cross-striated chicken muscle.

Strehler¹,

Pelloni²,

Heizmann³

et al. 1980

The Journal of Cell Biology

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“…There is, however, still considerable lack of knowledge regarding the sequence of appearance and organization of the myofibrillar structures during development (1,13,19,37,49). One of the major transverse structures in a mature cross-striated muscle fiber, the Z-band, has been described as the initial site of myofibrillogenesis (19), whereas the second one, the so-called M-line, has only recently been found to play a role in the organization of the assembly of the myofibrillar structure (10,12,16,43). THE Our own investigations on the structure and function of the M-line region ofchicken skeletal and heart muscle indicate the presence of two major protein components: the muscle type isoprotein of creatine kinase (MM-CK) (48,50,52) and the 165,000 M-protein (42,43).…”

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confidence: 99%

The Mr 165,000 M-protein myomesin: a specific protein of cross-striated muscle cells.

Eppenberger¹,

Perriard²,

Rosenberg³

et al. 1981

The Journal of Cell Biology

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The tissue specificity of chicken 165,000 M-protein, tentatively named "myomesin," a tightly bound component of the M-line region of adult skeletal and heart myofibrils, was investigated by immunological techniques . Besides skeletal and heart muscle, only thymus (known to contain myogenic cells) was found to contain myomesin . No myomesin could, however, be detected in smooth muscle or any other tissue tested . This result was confirmed in vitro on several cultured embryonic cell types. Only skeletal and heart muscle cells, but not smooth muscle or fibroblast cells, showed the presence of myomesin . When the occurrence and the distribution of myomesin during differentiation of breast muscle cells in culture were studied by the indirect immunofluorescence technique, this protein was first detected in postmitotic, nonproliferating myoblasts in a regular pattern of fluorescent cross-striations . In electron micrographs of sections through young myotubes, it could be shown to be present within the forming H-zones of nascent myofibrils . In large myotubes the typical striation pattern in the M-line region of the myofibrils was observed . Synthesis of myomesin measured by incorporation of [31S] methionine into immunoprecipitable protein of differentiating cells increased sharply after -48 h in culture, i .e ., at the time when the major myofibrillar proteins are accumulated . No significant amounts of myomesin were, however, found in cells prevented from undergoing normal myogenesis by 5'-bromodeoxyuridine .The results indicate that myomesin (a) is a myofibrillar protein specific for cross-striated muscle, (b) represents a highly specific marker for cross-striated muscle cell differentiation, and (c) might play an important role in myofibril assembly and/or maintenance.The temporal appearance of myofibrillar proteins as well as the composition and organization of myofibrils in differentiating muscle cells have been subjects of intense studies in recent years (for review, see references 1, 5, 11, 13, 17, 19, 24, and 30) . Investigations of the properties of a number ofnewly detected, so-called minor components of the myofibrillar compartment (12,14,25,28,31,48,53) have provided a better insight into the molecular organization of the unit of contractility, the sarcomere . There is, however, still considerable lack of knowledge regarding the sequence of appearance and organization of the myofibrillar structures during development (1,13,19,37,49). One of the major transverse structures in a mature cross-striated muscle fiber, the Z-band, has been described as the initial site of myofibrillogenesis (19), whereas the second one, the so-called M-line, has only recently been found to play a role in the organization of the assembly of the myofibrillar structure (10,12,16,43 Our own investigations on the structure and function of the M-line region ofchicken skeletal and heart muscle indicate the presence of two major protein components: the muscle type isoprotein of creatine kinase (MM-CK) (48, 50, 52) and the 165...

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Table 7.IV

Yang¹,

Wu²,

Böhm³

Landolt-Börnstein - Group VII Biophysics

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Isolation, purification and characterization of creatine kinase from bovine cardiac muscle

Cited by 15 publications

References 22 publications

Biochemical and ultrastructural aspects of Mr 165,000 M-protein in cross-striated chicken muscle.

Biochemical and ultrastructural aspects of Mr 165,000 M-protein in cross-striated chicken muscle.

The Mr 165,000 M-protein myomesin: a specific protein of cross-striated muscle cells.

Table 7.IV

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