By Alton Meister
Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative studies of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unequalled view of the historic improvement of enzymology. The sequence bargains researchers the newest figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic procedure, and their software in either the laboratory and undefined. each one quantity within the sequence gains contributions via top pioneers and investigators within the box from all over the world. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of issues and lengthy historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally via any scientist drawn to the invention of an enzyme, its homes, and its applications.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 59
The interaction of CSAT antigen with fibronectin can also be inhibited by the fibronectin cell-binding tetrapeptide. A Kd of lo-' M has been estimated for the interaction of CSAT antigen 46 STEVEN K. AKIYAMA A N D KENNETH M . K. M. Yamada, unpublished data). The estimated value of Kd = 2 x M for the interaction of CSAT with the fibronectin tetrapeptide is consistent with the value estimated for the interaction of the peptide with intact cells in inhibition assays (102). A nine amino acid peptide from an irrelevant portion of the fibronectin molecule has no effect on the interaction of CSAT antigen and fibronectin (151).
13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 9. 10. Tyr-Ala-Val-Thr-G1y-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys 3. Val-Thr-Gly-Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Cys 4. Gly-Arg-Gly-Asp-Ser-Pro-Cys 5. Gly-Arg-Gly-Asp-Ser 6. Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro --Arg-Gly-Asp-Ser-Pro-Ala-Cys 7. Arg-Gly-Asp-Ser a. TABLE V Synthetic Peptides with Fibronectinlike Activities for Platelets" 34 STEVEN K. AKIYAMA AND KENNETH M. YAMADA fibrinogen substrates (127,128). The inhibition of direct fibrinogen binding is interesting because even at high concentrations of peptide, inhibition is incomplete, indicating that the peptide acts to lower the apparent affinity of fibrinogen for its receptor (128).
J . Cell. , 27, 189-203 (1985). 15. , Ann. Rev. , I, 67-90 (1985). 16. , Ann. Rev. , 1, 91-113 (1985). 17. L. , Alan R. Liss, New York, 1985, pp. 89-121. 18. , J. Cell. , 28, 79-97 (1985). 19. J. , in Rheumarology, K. Kuhn and T. , Karger, Basel, 1985. 20. , Fibronectin, Academic, New York, in press. (1986). K. , Comp. Biochem. Physiol. B , 76,687-694 (1983). 22. , Hybridoma, 1, 99-108 (1982). 52 STEVEN K . AKIYAMA AND KENNETH M. YAMADA 23. M. , J . ,80, 492-498 (1979). 24. , Biochemistry, 16, 5552-5559 (1977).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 59 by Alton Meister