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Building) and it remains the tallest in Paris It is so sound that it never sways more than 7 cm (2.5 in) in strong winds THINGS TO DO THERE Visit the information area on the first floor to get the history of the tower Enjoy the beautiful view of Paris from the second floor Explore the top level with some more breathtaking views of Paris. Paris Agreement The Parties to this Agreement, Being Parties to the United Nations Framework Convention on Climate Change, hereinafter referred to as “the Convention”, Pursuant to the Durban Platform for Enhanced Action established by decision 1/CP.17 of the Conference of the Parties to the Convention at its seventeenth session. Brede's Accordion MIDI File Collection: New MIDIS and Music sheet: After you've gone - MIDI-37kb - After you've gone - PDF-69kb. And the Angel sing - MIDI-37kb - And the Angel singu - PDF-69kb. Careless Hands - MIDI-37kb - Careless Hands - PDF-197kb. Come September - MIDI-32kb - Come September - PDF-17kb. Confessin - MIDI-21kb - Confessin - PDF. Feb 14, 1998 Stanley Karnow is also the author of Paris in the Fifties, published by Three Rivers Press. Purchase a Download Paris in the Fifties. MP3 audio - Standard Price: $0.99. Request Download. Join our community of free eBook lovers! Choose from our hand picked collection of the best public domain books to be found in the English language from the last five hundred years. Register now for free access to our ebooks, all available as EPUB and Kindle MOBI books. All ebooks are provided without DRM protection and can be read.

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Biochimie 70 (1988) 1131 - 1135 (~) Socirt6 de Chimie biologique/Elsevier, Paris
Limited proteolyses in pancreatic chymotrypsinogens and trypsinogens Mireille R O V E R Y Centre de Biochimie et de Biologie mol(culaire du CNRS, B.P. 71, 13402 Marseille Cedex 9, France (Received 6-11-1987, accepted 2-12-1987)
Summary - - In the 1950's, the specific cleavages of the peptide bonds occurring in bovine cationic chymotrypsinogen and trypsinogen were among the first examples of limited proteolyses. According to the split bond(s), the precursor is transformed into enzyme or different forms of zymogen or again into inert protein. The conversion of trypsinogen into trypsin triggers the activations of all the other enzyme precursors of pancreatic juice. In the pancreas, several factors oppose try'psinogen autoactivation, whereas, in the duodenum, all the conditions are favorable for trypsinogen activation by enteropeptidase. chymotrypsinogen / trypsinogen / enzyme precursor activation / limited proteolysis / pancreatic juice
Bovine chymotrypsinogen A (cationic form)
The studies on chymotrypsinogens and trypsinogens initiated by Professor Desnuelle in the early fifties were particularly oriented by the works ot Northrop, Kunitz and Herriott on crystalline cn~',mes,~ [1] and by those of Jacobsen on the activation of bovine chymotrypsinogen A [2]. The years 1945-1950 saw the arrival of new methods for determining primary structures of polypeptides such as: characterizations of the N-terminal groups (Sanger) and N-terminal sequence (Edman), chromatographic separations of proteins, peptides and amino acids, together with the analyses of the amino acid compositions of polypeptides (Stein and Moore). These techniques, although having become sophisticated with the use of miniaturization and automation, remain nevertheless in their concept the basis of protein chemistry. Nowadays, it is often found more convenient to deduce the protein sequence from the corresponding nucleotide sequence if some information on the protein structure is available. However, the protein c:hemistry methods are essential for determinations of S - S bridges, functional amino acids and structural domains.
In the middle of the twentieth century, crystallization was considered as the best method for protein purification. Chymotrypsinogen A and chymotrypsin a, which could be easily crystallized, were especially studied. As chymotrypsin ~t was shown to contain two extra N-terminal [3] and two extra C-terminal groups [4], compared to the single N- and C-terminal end groups of chymotrypsi,~ogen A, the formation of chymotrypsin by limited proteolysis of chymotrypsinogen was definitely proven. The enzyme precursor is activated by a single tryptic bond cleavage [5]. Chymotrypsin autolysis then occurs by splitting other peptide bonds (maximum 3). Different chymotrypsins are formed depending upon the number of cleavages (Fig. 1) [6]. On the other hand, when chymotrypsinogen only undergoes chymotrypsin hydrolysis, 1, 2 or 3 peptide bonds are split giving rise to the formation of inactive yet activatable neochymotrypsinogens (Fig. i) [6]. The separation of the three chains of chymotrypsin ~t, following S - S bridge cleavages [7-9], contributed to the establishment of the amino acid sequence of chymotrypsinogen A [10, 11].
M. Rovery
bovine c h y m o t r y p s i n o g e n A
The two areas in which proteolytic cleavages take place : 10 11 12 13 14 15 16 17 Leu. Set,.Gly. Leu. Set, Arg. lle.Val..
144 145 146 147 148 149 150 Thr. Arg. Tyr. Thr. Asn. Ala. Asn...
tryptic activation
a chymotrypsin proteolysis
1, chymotrypsin
245[ I (fast) + chymotrypsin autolysis
14 1 [
6 chymotrypsin + Ser.Arg
116 Leu
1461 Tyr
(slow) + chymotrypsin autolysis + (NH4)2SO4 a chymotrypsin + Thr.Asn
1,6 Leu
,461 Tyr
24 1
Tyr Thr a c h y m o t r y p s i n p r o t e o l y s i s + (NH4)2SO 4
1149 Ala
245]+ T h r . A s n
C c h y m o t r y p s i n p r o t e o l y s i s + (NH4)2SO 4
,31114 Leu
Fig. 1. Limited proteolyses of bovine chymotrypsinogen A resulting in the formation of chymotrypsins or neochymotrypsinogens.
The activating cleavage occurs on the 15th peptide bond of the precursor polypeptide chain (Fig. 1). If the activation is performed in the presence of chymotrypsin inhibitor, the 13th bond will not be broken and the pentadecapeptide chain (A prime chain) will be obtained after S - S bond cleavages. When new enzyme precursors were to be characterized, the determination of the primary structure of a short chain was easier than that of the N-terminal sequence of the chymotrypsinogen. It must not be overlooked that at that time there was no automatic sequencer available.
nal sequences of these 6 proteins demonstrate that they belong to the chymotrypsinogen family [13]. In bovine pancreas, chymotrypsinogens A and B were studied in depth [14]. The third chymotrypsinogen is the subunit II of the trimer complex pro-carboxypeptidase A [15]. In porcine pancreas, three chymotrypsinogens were also found: A, B and C [16, 17]. Chymotrypsinogen C has an N-terminal sequence resembling that of subunit II buL unlike the latter, the porcine precursor is not included in a protein complex.
Bovine cationic trypsinogen Different forms of chymotrypsinogens The chromatographic pattern of the proteins contained in pancreatic juice showed that most of them are enzymes or enzyme precursors [12]. In Fig. 2, the protein separation profiles of bovine and porcine pancreatic juices are compared [13]. The three hatched areas in each profile indicate the fractions which, after trypsin activation, hydrolyze the chymotrypsin substrate, acetyltyrosine ethyl ester. In Fig. 3, the N-termi-
Before Professor Desnuelle's group started investigating trypsinogen activation, it had already been observed [1] that: 1) the transformation of trypsinogen into trypsin can be carried out either with a minute amount of trypsin (autoactivation) or with an intestinal enzyme, enterokinase, or yet again with a penicillium kinase; 2) when using a very dilute trypsinogen solution, the rate of activation by trypsin is negligible compared to that with enterokinase; 3) the autocatalytic reaction does not provide a full
Proteolyses in chymotrypsinogens and trypsinogens RC50
yield of trypsin due to the formation of some inert proteins; 4) in vitro the presence of calcium (20 mM) hastens the autoactivation and inhibits the formation of inert proteins; 5) a trypsin inhibitor is present in pancreatic juice. All the above findings of the beginning of the century were later confirmed, improved and expanded. The determination of the N-terminal amino acids of bovine cationic trypsinogen and its related enzyme was undertaken in Marseilles. In order to eliminate and also to prevent autodigestion products, diisopropylphosphoryl trypsin crystals were used. A single N-terminal group was found in each protein: Val in trypsinogen and Ile in trypsin [3]. Study of the dinitrophenyl peptides resulting from a limited HCl-hydrolysis of the dinitrophenyl proteins, led to the elucidation of a short length of the N-terminal sequence: Val - ( A s p ) 4 - Lys for trypsinogen and I l e - V a l - G l y for trypsin [18]. At the same time, Neurath's group showed that a hexapeptide V a l - ( A s p ) 4 - L y s is cut off during the conversion of trypsinogen into trypsin and that the peptide liberation is concomitant with the appearance of trypsin activity [19]. Given all the above results, it was suggested that the trypsinogen Nterminal sequence would be: V a l - ( A s p ) 4 L y s - I l e - V a l - G l y and that the activating cleavage would occur on the Lys6-Ile 7 bond. This hypothesis was confirmed in the course of trypsinogen sequence elucidation [20~ 21].
Bovine pancreatic juice
p H 6.0
DEAE-cellulose Tg
pH 8.0
A Chtg B ProCpA Chtg A I ~STi .. A ~. [ ~ ProCpB L=pase/ , ~ RNase
Amylase ~
%/' 7//
Porcine pancreatic juice
pH 4.3
p.H 6.0
T g /
ProCpA ~ ProCpB B2 /
Lipase DNase,V//,
Fig. 2. Chromatography of bovine and porcine juices on an
anion- and a cation-exchange column. The dialyzed juice is first chromatographed at pH 8.0 on DEAE-cellulose. The unretarded proteins (the so-called cationic proteins) are
separated latr.r on a cation-exchanger (CM-cellulose or IRC 50). The anionic proteins retained by the DEAE-cellulose are eluted by a slow increase of the ionic strength of the buffer. The hatched areas represent the fractions in which an ATEE-splitting activity is found after tryptic activation.
Sequence N ° . Chymotrypsinogen
1 • 2
T l
Bovine chymotrypsinogen A
Cgs-Gly-Val-Pro-Ala- I le-Gln-Pro-Val-Leu-Ser-Gly-Leu-Ser-Arg -tI le-Val
Bovine chymotrypsinogen
Cys-Gly-Val-Pro-Ala- I le-Gln-Pro-Val- Leu-Ser-Gly-Leu-Ala-Arg#-Ile-Val T!
T! B
Porcine chymotrypsinogen A
Cys- Gly-Va l-Pro-Ala- I le- Pro-Pro-Val- Leu-Ser-Gly- Leu-Ser-Arg -tI le- Val T
Porcine chymotrypsinogen B
Porcine chymotrypsinogen C
Cys-Gly-Val-Pro-Ala-Ile-Pro-Pro-Val-Leu-Ser-Gly-Leu-Ser-Arg~Ile-Val T Cys-Gly-Val-Pro-Ser-Phe-Pro-Pro-Asn-Leu-Ser-
Ala-Arg ~Val-val
Cys-Gly-Ala-Pro- I le- Phe-Gln-Pro-Asn-Leu-Ser-
T Bovine Subunit II (Bovine chymotrypsinogen C)
Fig. 3. N-terminal sequence of bovine and porcine chymotrypsinogens. The activation of each chymotrypsinogen was
performed in the presence of chymotrypsin inhibitor. The A prime chain was isolated after oxidation and its primary structure was determined. This chain is made up of 15 amino acid residues for chymotry.psinogensA and B and only 13 for chymotrypsinogens C. The invariant residues are in italics. T: activatingcleavages by trypsin.
M. Rovery
If the trypsin cleavages are not specifically oriented, they can abrogate part of the activation process. In the absence of calcium, 50% of trypsinogen molecules are cleaved on basic bonds other than the Lys-Ile bond and cannot be activated later on [22]. Likewise, the trypsin autolysis inconveniently occurs in the absence of calcium in particular. The splitting of the Arg~°5-Val t°6 bond or Lysl31-SerB2 bond does not lead to activity loss [23, 24], whereas if the cleavage of Lysl76-Asp 177 follows that of Lys131-Ser~32 bond, the resulting three-chain pseudo-trypsin exhibits a very weak affinity for trypsin substrates but an equal affinity for chymotrypsin substrates [25]. The role of calcium in the autoactivation of trypsinogen was better understood when it was shown that the zymogen possesses two binding sites for Ca 2÷, o n e with high affinity preventing the formation of inert proteins and also existing in trypsin (calcium concentration = 4 mM), and the other with a lower affinity speeding up the cleavage of the Lys-Ile bond by trypsin (calcium concentration, 50 mM) [26]. All the above findings and the data obtained in the studies of enteropeptidase (modern name for enterokinase) [27-29] threw light on the process of zymogen activations in vivo. Two facts prevent the premature activation of the enzyme precursors which would lead to pancreas destruction: 1) the presence in pancreatic juice of trypsin inhibitor which would neutralize a small amount of trypsin; 2) the negative charges ~4~
~-1.. .
,a~ t n ~ ;
tyl [~ltaUes



strategic linkage
which do not favor trypsin hydrolysis (the calcium concentration being only equal to 2 mM). The activation of trypsinogen is performed in the duodenum by enteropeptidase, an enzyme synthesized by the duodenal mucosa. The binding site of enteropeptidase recognizes the (Asp)4Lys structural unit and this specialized enzyme is the best activator for trypsinogen. The trypsin thus obtained activates all the other pancreatic precursors.
Different forms of trypsinogen Furthermore, Desnuelle's group studied the cationic form of porcine trypsinogen and the anionic forms of bovine and porcine precursors [30-32]. The latter, which are the most anionic proteins of pancreatic juices, were not found in the first investigations (Fig. 2), probably on account of their low chromatographic yields. It
is interesting to note that the activation of these anionic trypsinogens is much faster than that of the cationic zymogens. The N-terminal sequences of these three trypsinogens are as follows: Phe - Pro - T h r - ~' porcine cationic trypsinogen (Asp)a- Lys - lie - Val L porcine anionic trypsinogen P h e - P r o - T h r - ( A s p ) a - L y s '~ 2 bovine anionic S e r - (Asp) 4- Lys f trypsinogens Trypsinogens of many different species were also studied in other laboratories. The pattern (Asp)4-Lys is common in all these pancreatic precursors.
Acknowledgment I am grateful to Mrs. Vera Stefani-Martin for reviewing the English text.
References 1 Northrop J.H., Kunitz M. & Herriot R.M. (1948) in: Crystalline Enzymes 2nd edn., Columbia University Press, New York, pp. 96-167 2 Jacobsen C.F. (1947) C. R. Tray. Lab. Carlsberg Ser. Chim. 25,325-437 3 Rovery M., Fabre C. & Desnuelle P. (1953) Biochim. Biophys. Acta 12,547-559 4 Gladner J.A. & Neurath H. (1953)J. Biol. Chem. 205,345-352 5 Rovery M., Poilroux M., Curnier A. & Desnuelle P. (1955) Biochim. Biophys. Acta 17,565-578 6 Rovery M., Poilroux M., Yoshida A. & Desnueile P. (1957) Biochim. Biophys. Acta 23, 608-620 7 Meedom B. (1956) Acta Chem. Scand. 10, 881-882 8 Dinh Van Hoangl Rovery M., Guidoni A. & Desnuelle P. (1963) Biochim. Biophys. Acta 69, 188-190 9 Maroux S. & Rovery M. (1966) Biochim. Biophys. Acta 113, 126-143 10 Hartley B.S. & Kauffman D.L. (1966) Biochem. J. 101,229-231 11 Blow D.M., Birktoft J.J. & Hartley B.S. (1969) Nature 221,337-340 12 Keller P.J., Cohen E. & Neurath H. (1958)J. Biol. Chem. 233,344-349 13 Desnuelle P., Gratecos D., Charles M., Peanasky R., Baratti J. & Rovery M. (1970) in: Structure-Function Relationships of Proteolytic Enzymes (Desnuelle P., Neurath H. & Ottesen M., eds.), Copenhagen, pp. 21-34 14 Guy O., Gratecos D , Rovery M. & Desnuelle P. (1966) Biochim. Biophys. 'Acta 115,404-422
Proteolyses in chymotrypsinogens and trypsinogens 15 Peanasky R.J., Gratecos D., Baratti J. & Rovery M. (1969) Biochim. Biophys. Acta 181, 82-92 16 Charles M., Gratecos D., Rovery M. & Desnuelle P. (1967) Biochim. Biophys. Acta 140, 395-409 17 Gratecos D., Guy O., Rovery M. & Desnuelle P. (1969) Biochim. Biophys. Acta 175, 82-96 18 Desnuelle P. & Fabre C. (1955) Biochim. Biophys. Acta 18, 49-57 19 Davie E.W. & Neurath H. (1955) J. Biol. Chem. 212, 515-529 20 Walsh K.A., Kauffman D.L. & Neurath H. (1962) Biochemistry 1,893-898 21 Walsh K.A., Kauffman D.L., Kumar K.S.V.S. & Neurath H. (1964) Proc. Natl. Acad. Sci. USA 51,301-308 22 Gabeloteau C. & Desnuelle P. (1958) Bull. Soc. Chim. Biol. 40, 35-43 23 Maroux S. & Desnuelle P. (1969) Biochim. Bio-
phys. Acta 181, 59-72 24 Schroeder D.D. & Shaw E. (1968) J. Biol. Chem. 243, 2943-2949 25 Smith R.L. & Shaw E. (1969) J. Biol. Chem. 244, 4704-4712 26 Delaage M. & Lazdunski M. (1967) Biochem. Biophys. Res. Commun. 28, 390-394 27 Maroux S., Baratti J. & Desnuelle P. (1971) J. Biol. Chem. 246, 5031- 5039 28 Louvard D., Maroux S., Baratti J. & Desnuelle P. (1973) Biochim. Biophys. Acta 309, 127-137 29 Baratti J., Maroux S., Louvard D. & Desnuelle P. (1973) Biochim. Biophys. Acta 315,147-161 30 Charles M., Rovery M., Guidoni A. & Desnuelle P. (1963) Biochim. Biophys. Acta 69, 115-129 31 Puigserver A. & Desnuelle P. (1971) Biochim. Biophys. Acta 236, 499-502 32 Louvard M.N. & Puigserver A. (1974) Biochim. Biophys. Acta 371,177-185

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