Translation of "Ficin" in German

The arteries are placed in a measuring cylinder and the clear ficin solution is poured over them.

Cysteine proteases are, for example, papain, bromelain or ficin.

The arteries are now ready for sterilisation or for hydrolysis with ficin, papain or the like.

The arteries are placed in a measuring cylinder and the ficin solution described above is poured over them.

They are now ready for hydrolysis with ficin, papain or another suitable enzyme.

The extract contains effective amounts of the proteolytic ficin enzyme and contributes to cell regeneration.

The latter originate in the main from animal organs or parts thereof (for example the carotid arteries of calves or cardiac valves from pigs), which after removal are freed, by means of an enzymatic hydrolysis (for example with ficin), from proteins which potentially act as antigens.

It has now been found, surprisingly, that by means of novel intermolecular and/or intramolecular crosslinking of the macromolecules of the intercellular matrix of organs or parts of organs, prior to or even without the proteolytic degradation by means of ficin, the biophysical characteristics originally present, such as, for example, in the case of vascular prostheses, the axial and radial elasticity and the smooth nature of the inner surface of the vessels, are substantially retained.

In place of the abovementioned treatment with said aldehyde, the matrix can, in another (alternative) additional process stage, be freed from material which potentially acts as an antigen, by hydrolytic degradation with ficin, papain or another protease of the same or similar substrate specificity.

If the said proteolysis with ficin, papain or the like is carried out, individual amino groups are liberated in the intercellular matrix.

However, with organs pre-treated in this way, such as, for example, vascular prostheses (U.S. Pat. No. 3,093,439, U.S. Pat. No. 4,120,649 or Swiss Pat. No. 595,105) it has been found that the biophysical characteristics originally present, such as the elasticity in the axial and radial directions and also the extremely smooth nature of the inner surface of the vessels, are completely lost as a result of the enzymatic degradation by means of ficin.

The preferred second stage of the process thus comprises an incubation of the organ material in a solution, appropriately an aqueous solution, of ficin, papain or another protease of the same or similar substrate specificity.

It is advantageous subsequently to treat the crosslinked product with a dialdehyde, in order to bind amino groups which have not reacted, or to free the crosslinked product from material which potentially may act as an antigen, by hydrolysis with ficin, papain or a protease having a smaller action.

The starting peptides can be obtained by reductive cleavage of N-Boc-protected polymyxin B, for example using metal hydrides, for example NaBH4 or NaCNBH3, or by enzymatic cleavage, for example with the protease ficin, which is known from the literature.

Proteolytic enzymes, such as trypsin, chymotrypsin, papain, ficin, and bromelain as well as subtilisin, which is obtained from bacteria, are particularly well suited for the decomposition of necrotic tissue.

As described in Example 7, calf carotid arteries are first crosslinked with adipic acid chloride in tetrahydrofuran and then subjected to hydrolysis with ficin.

The pericardia crosslinked with adipic acid chloride are immersed in a ficin solution as described in Example 7 or 8.

As described in Example 7 or 8, calf carotid arteries are first crosslinked with adipic acid chloride in tetrahydrofuran and then subjected to hydrolysis with ficin.

Arteries, which--as described in Example 7 or 8--have been crosslinked with adipic acid chloride and hydrolysed with ficin, are then placed in the suspension of aldehyde starch obtained above.

Examples of endopeptidases include pepsin, trypsin, chymotrypsin, collagenase, papain, ficin, clostripain, subtilisin, elastase and bromelain and numerous others.

These enzymes, which catalyse the cleavage of the peptide bond, include for example acrosin, aminopeptidase B, bromelain, calpain I, carboxypeptidase A, cathepsin A, cathepsin B, cathepsin D, cathepsin E, cathepsin K, chymotrypsin, collagenase, dipeptidyl peptidase 4, Dispase, elastase, factor IIa, factor Xa, ficin, gpr-endopeptidase, kallikrein, MBTPS1, papain, plasmin, Prepilin type IV peptidase, prolyl-oligopeptidase, proteinase K, proteasome, renin, secretases (alpha-, beta- and gamma-secretase), thermolysin, thrombin, and urokinase.

In the embodiments in which the proteolytic agent is a protease, it in principle can be selected from all proteases obtained recombinantly from eukaryotes or prokaryotes or obtained endogenously from organisms or organism constituents from serine, threonine, cysteine, asparagine, metal or unknown type, like for example acrosin, aminopeptidase B, bromelain, calpain I, carboxypeptidase A, cathepsin A, cathepsin B, cathepsin D, cathepsin E, cathepsin K, chymotrypsin, collagenase, dipeptidyl peptidase 4, dispase, elastase, factor IIa, factor Xa, ficin, gpr-endopeptidase, HIV-protease, kallikrein, MBTPS1, bromelain, papain, pepsin, plasmin, prepilin type IV peptidase, prolyl-oligopeptidase, proteinase K, proteasom, renin, seccretases (alpha-, beta- and gamma-secretase), thermolysin (EC 3,4,24,27), thrombin, trypsin, urokinase, protease N from Bacillus sp., protease P from Aspergillus sp., protease XIV from Streptomyces sp, and protease S from Bacillus stearothermophilus.

It has been found especially suitable to perform the proteolysis in the presence of ficin and L-cysteine whereby one uses preferably an aqueous solution at a pH-value of about 5.5 to about 6.5 and especially 6, and at a temperature of 30° to 50° C., especially at about 37° C. The adjustment of the pH-value is performed adequately by adding 1N trisodiumcitrate buffer.