![]()
|
|
||||||||
From the
1 From the Biology Department, Brookhaven National Laboratory, Upton, New York 11973
The tryptic peptides of bovine pancreatic secretory trypsin inhibitor (Greene, L. J., and Giordano, J. S., Jr., J. Biol. Chem., 244, 285 (1969)) have been ordered in a unique sequence by a series of specific chemical and limited enzymatic cleavages of the performic acid-oxidized derivative. The amino acid sequence is [see PDF for sequence].
The Structure of the Bovine Pancreatic Secretory Trypsin InhibitorKazal's Inhibitor
II. THE ORDER OF THE TRYPTIC PEPTIDES
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
D. R. Hewett, A. L. Simons, N. E. Mangan, H. E. Jolin, S. M. Green, P. G. Fallon, and A. N.J. McKenzie Lethal, neonatal ichthyosis with increased proteolytic processing of filaggrin in a mouse model of Netherton syndrome Hum. Mol. Genet., January 15, 2005; 14(2): 335 - 346. [Abstract] [Full Text] [PDF] |
||||
![]() |
H.-J. Magert, L. Standker, P. Kreutzmann, H.-D. Zucht, M. Reinecke, C. P. Sommerhoff, H. Fritz, and W.-G. Forssmann LEKTI, a Novel 15-Domain Type of Human Serine Proteinase Inhibitor J. Biol. Chem., July 30, 1999; 274(31): 21499 - 21502. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |