TY - JOUR
T1 - Studies on contractile proteins in ADP- and collagen-induced platelet aggregation
AU - Muhlrad, A.
AU - Kornberg, A.
AU - Werber, M. M.
N1 - Funding Information:
This work was supportedb y a grant from the Israel Coanissim for Basic Reeearch to A.M. We thank the let8 ProfessorG .Izak for continuous encouragem8nt.W e are gratefult o S. Argaman and N. Furst for excellentt ech-nical assistance.
PY - 1981
Y1 - 1981
N2 - Human platelets were induced to aggregate by either ADP or collagen. Both aggregated and non-aggregated (resting) platelets were then washed twice, lyzed by osmotic shock in the presence of several protease inhibitors and fractionated. The cytoplasmic fraction (Fraction I) was separated from the rest of the cell by centrifugation, the pellet was suspended in 0.8 M KC1 and the extract (Fraction II) was separated from the particulate fraction (Fraction III). The relative amounts of three contractile proteins, myosin, actin and actin-binding protein were evaluated and the activities of myosin, K+-(EDTA)-activated ATPase, and of actomyosin, Mg2+-mediated ATPase, were determined in all fractions. Following ADP- or collagen-induced aggregation the specific activities of both myosin and actomyosin ATPases increased significantly in the non-soluble Fraction III.
AB - Human platelets were induced to aggregate by either ADP or collagen. Both aggregated and non-aggregated (resting) platelets were then washed twice, lyzed by osmotic shock in the presence of several protease inhibitors and fractionated. The cytoplasmic fraction (Fraction I) was separated from the rest of the cell by centrifugation, the pellet was suspended in 0.8 M KC1 and the extract (Fraction II) was separated from the particulate fraction (Fraction III). The relative amounts of three contractile proteins, myosin, actin and actin-binding protein were evaluated and the activities of myosin, K+-(EDTA)-activated ATPase, and of actomyosin, Mg2+-mediated ATPase, were determined in all fractions. Following ADP- or collagen-induced aggregation the specific activities of both myosin and actomyosin ATPases increased significantly in the non-soluble Fraction III.
KW - ADP and collagen aggregation
KW - platelet contractile proteins
UR - http://www.scopus.com/inward/record.url?scp=0019455762&partnerID=8YFLogxK
U2 - 10.1016/0049-3848(84)90042-2
DO - 10.1016/0049-3848(84)90042-2
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AN - SCOPUS:0019455762
SN - 0049-3848
VL - 21
SP - 147
EP - 156
JO - Thrombosis Research
JF - Thrombosis Research
IS - 1-2
ER -