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Antigenic Probes Locate a Serum-gelsolin-interaction Site on the C-terminal Part of Actin

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Journal Biochem J
Specialty Biochemistry
Date 1987 Dec 1
PMID 2449166
Citations 8
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Abstract

The implication of part of the C-terminal of actin (within the 285-375 sequence) in the interaction of serum gelsolin was investigated by the use of specific antibodies. These antibodies were directed against two or three discrete epitopes, one of which was specific for skeletal-muscle actin. Some of these epitopes were found to be near the serum gelsolin-actin interface. Thus it can be assumed that part of the C-terminal of actin is exposed at the barbed end of the actin filament. The interaction between tropomyosin and actin was also studied.

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References
1.
Benyamin Y, Roger M, Gabrion J, Robin Y, van THOAI N . Immunological comparison of muscle actins from mammal, bird and fish: a quantitative approach. FEBS Lett. 1979; 102(1):69-74. DOI: 10.1016/0014-5793(79)80930-8. View

2.
Janmey P, Stossel T, Lind S . Sequential binding of actin monomers to plasma gelsolin and its inhibition by vitamin D-binding protein. Biochem Biophys Res Commun. 1986; 136(1):72-9. DOI: 10.1016/0006-291x(86)90878-8. View

3.
Sutoh K, Hatano S . Actin-fragmin interactions as revealed by chemical cross-linking. Biochemistry. 1986; 25(2):435-40. DOI: 10.1021/bi00350a024. View

4.
Sutoh K . Actin-actin and actin-deoxyribonuclease I contact sites in the actin sequence. Biochemistry. 1984; 23(9):1942-6. DOI: 10.1021/bi00304a009. View

5.
Janmey P, Stossel T . Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin. J Muscle Res Cell Motil. 1986; 7(5):446-54. DOI: 10.1007/BF01753587. View