Abstract
Specific extraction of Z bands, intercalated disks and desmosomes was accomplished with molar concentrations of urea. Thick and thin filaments and M line material were undisturbed, demonstrating that the Z band protein is not similar to actin, myosin, or the M-line protein. The literature indicates that the tropomyosins are the only other structural proteins present in sufficient amounts to account for the extracted Z bands. However, the evidence for a lipid-protein association in the Z bands is considered and is further supported by the close association of the dense material of the Z bands, intercalated disks, and desmosomes with the lipoprotein cell membranes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 181-189 |
| Number of pages | 9 |
| Journal | Journal of Ultrasructure Research |
| Volume | 24 |
| Issue number | 3-4 |
| State | Published - Aug 1968 |
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ASJC Scopus subject areas
- Anatomy
- Molecular Biology
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Urea extraction of Z bands, intercalated disks, and desmosomes. / Rash, John E.; Shay, Jerry W.; Biesele, John J.
In: Journal of Ultrasructure Research, Vol. 24, No. 3-4, 08.1968, p. 181-189.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Urea extraction of Z bands, intercalated disks, and desmosomes
AU - Rash, John E.
AU - Shay, Jerry W.
AU - Biesele, John J.
PY - 1968/8
Y1 - 1968/8
N2 - Specific extraction of Z bands, intercalated disks and desmosomes was accomplished with molar concentrations of urea. Thick and thin filaments and M line material were undisturbed, demonstrating that the Z band protein is not similar to actin, myosin, or the M-line protein. The literature indicates that the tropomyosins are the only other structural proteins present in sufficient amounts to account for the extracted Z bands. However, the evidence for a lipid-protein association in the Z bands is considered and is further supported by the close association of the dense material of the Z bands, intercalated disks, and desmosomes with the lipoprotein cell membranes.
AB - Specific extraction of Z bands, intercalated disks and desmosomes was accomplished with molar concentrations of urea. Thick and thin filaments and M line material were undisturbed, demonstrating that the Z band protein is not similar to actin, myosin, or the M-line protein. The literature indicates that the tropomyosins are the only other structural proteins present in sufficient amounts to account for the extracted Z bands. However, the evidence for a lipid-protein association in the Z bands is considered and is further supported by the close association of the dense material of the Z bands, intercalated disks, and desmosomes with the lipoprotein cell membranes.
UR - http://www.scopus.com/inward/record.url?scp=0014317442&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0014317442&partnerID=8YFLogxK
M3 - Article
C2 - 4883856
AN - SCOPUS:0014317442
VL - 24
SP - 181
EP - 189
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 3-4
ER -