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SMILLIE, L. B., FURKA, A., NAGABHUSHAN, N., STEVENSON, K. J., PARKES, C. O. (1968) Structure of Chymotrypsinogen B compared with Chymotrypsinogen A and Trypsinogen. Nature, 218 (5139). 343-346 doi:10.1038/218343a0

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Reference TypeJournal (article/letter/editorial)
TitleStructure of Chymotrypsinogen B compared with Chymotrypsinogen A and Trypsinogen
JournalNature
AuthorsSMILLIE, L. B.Author
FURKA, A.Author
NAGABHUSHAN, N.Author
STEVENSON, K. J.Author
PARKES, C. O.Author
Year1968 (April)Volume218
Issue5139
PublisherSpringer Science and Business Media LLC
DOIdoi:10.1038/218343a0Search in ResearchGate
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Mindat Ref. ID2565709Long-form Identifiermindat:1:5:2565709:0
GUID0
Full ReferenceSMILLIE, L. B., FURKA, A., NAGABHUSHAN, N., STEVENSON, K. J., PARKES, C. O. (1968) Structure of Chymotrypsinogen B compared with Chymotrypsinogen A and Trypsinogen. Nature, 218 (5139). 343-346 doi:10.1038/218343a0
Plain TextSMILLIE, L. B., FURKA, A., NAGABHUSHAN, N., STEVENSON, K. J., PARKES, C. O. (1968) Structure of Chymotrypsinogen B compared with Chymotrypsinogen A and Trypsinogen. Nature, 218 (5139). 343-346 doi:10.1038/218343a0
In(1968, April) Nature Vol. 218 (5139) Springer Science and Business Media LLC

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OLSON, M. O. J., NAGABHUSHAN, N., DZWINIEL, M., SMILLIE, L. B., WHITAKER, D. R. (1970) Primary Structure of α-Lytic Protease: a Bacterial Homologue of the Pancreatic Serine Proteases. Nature, 228 (5270). 438-442 doi:10.1038/228438a0
Matthews, B.W. (1968) Some crystal forms of bovine chymotrypsinogen B and chymotrypsinogen A. Journal of Molecular Biology, 33 (2). 499-501 doi:10.1016/0022-2836(68)90206-4
Šorm, F., Keil, B., Holeyšovský, V., Meloun, B., Mikeš, O., Vaněček, J. (1958) On proteins. XLIX. Comparison of the microstructures of chymotrypsinogen and trypsinogen. Collection of Czechoslovak Chemical Communications, 23. 985-988 doi:10.1135/cccc19580985
Morgan, P. H., Robinson, N. C., Walsh, K. A., Neurath, H. (1972) Inactivation of Bovine Trypsinogen and Chymotrypsinogen by Diisopropylphosphorofluoridate. Proceedings of the National Academy of Sciences, 69 (11) 3312-3316 doi:10.1073/pnas.69.11.3312
Walsh, K. A., Neurath, H. (1964) TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS. Proceedings of the National Academy of Sciences, 52 (4) 884-889 doi:10.1073/pnas.52.4.884
Keil, B., Šorm, F., Holeyšovský, V., Kostka, V., Meloun, B., Mikeš, O., Tomášek, V., Vaněček, J. (1959) On proteins. LVI. On the partial structures of bovine chymotrypsinogen and trypsinogen. Collection of Czechoslovak Chemical Communications, 24. 3491-3493 doi:10.1135/cccc19593491
HARTLEY, B. S. (1964) Amino-Acid Sequence of Bovine Chymotrypsinogen-A. Nature, 201 (4926). 1284-1287 doi:10.1038/2011284a0
Vaněček, J., Keil, B., Šorm, F. (1955) On proteins. XXVIII. Comparison of arginine peptides from partial hydrolysates of chymotrypsinogen and trypsinogen. Collection of Czechoslovak Chemical Communications, 20. 363-370 doi:10.1135/cccc19550363
JANKOVIĆ, B. D., ISAKOVIĆ, K., HORVAT, J. (1968) Bursa of Fabricius and Immunological Tolerance. Nature, 218 (5139). 379-380 doi:10.1038/218379a0
Smillie, Lawrence B., Hartley, Brian S. (1965) The disulphide bridges of chymotrypsinogen B. Journal of Molecular Biology, 12 (3). 933-936 doi:10.1016/s0022-2836(65)80341-2
GINSBORG, B. L. (1968) Effect of Bromide Ions on Junctional Transmission. Nature, 218 (5139). 363 doi:10.1038/218363a0
 
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