Pancreatic 0-kallikrein

Fukushima D, Kitamura N, Nakanishi S. Nucleotide sequence of cloned cDNA for human pancreatic kallikrein. Biochemistry 1985 24 8037-8043. 

The acyl derivatives of kallikiein were prepared from porcine pancreatic kallikrein. In our experiments we used benzoyl-kallikiein, By deacylation the enzymatically active kallikrein was generated in plasma from benzoy 1-kallikrein demonstrated by means of its amidolytic activity. From the time course of reactivation of benzoy 1-kallikrein, a half-time of reactivation of 54 minutes was calculated. Benzoyl- kallikrein was protected from being inactivated by plasma inhibitors. Therefore, the kallikrein activity in nlasma was hicher after incubation... 

KLK1 Pancreatic/renal kallikrein, hPRK M25629 M33105 Hs. 123107 SOI.160 Q07276... 

Fujimori H, Levison PR, Schachter M. Purification and partial characterization of cat pancreatic and urinary kallikreins—comparison with other cat tissue kallikreins and related proteases. Adv Exp Med Biol 1986 198(Pt A) 219-228. 

Petraki CD, Karavana VN, Revelos KI, Luo LY, Diamandis EP. Immunohistochemical localization of human kallikreins 6 and 10 in pancreatic islets. Histochem J 2002 34 313-322. 

Yousef GM, Borgono CA, Popalis C, et al. In-silico analysis of kallikrein gene expression in pancreatic and colon cancers. Anticancer Res 2004 24 43-51. 

Therapeutic Function Proteinase inhibitor Chemical Name Trypsin inhibitor, pancreatic basic Common Name Aprotinin Frey inhibitor Kallikrein-trypsin inhibitor Chemical Abstracts Registry No. 9087-70-1... 

Siegel M, Werner M. Allergische Pankreatitis bei einer SensibUisierung gegen den Kallikrein-Trypsin-Inaktivator. [Allergic pancreatitis caused by sensitization to the kalli-krein-trypsin inactivator.) Dtsch Med Wochenschr 1965 90(39) 1712-16. 

Affinity chromatographic removal of kallikrein from other 4-tosyl-L- 346 arginine methyl ester ( TAME ) esterases in human urine Purification and affinity chromatography of pancreatic 239... 

Figure 11. Organization of the exons encoding the serine protease domains of several proteins. Abbreviations used are the same as in the legend to Figure 4. References for the genes for the pancreatic proteases, kallikrein, nerve growth factors, haptoglobin and complement factor B can be found in reference 83. See text for the other references.

The pancreatic trypsin inhibitor binds to trypsin, chymotrypsin, plasmin, and kallikrein, but does not inhibit elastase and subtilisin. Model-building studies of the inhibitor chymotrypsin complex show that the enzyme and Inhibitor have highly complementary structures. If Lys-15 (in a non-protonated form) is placed in the spedficity pocket with the C and NH of Lys-15 in similar positions to those of tryptophan in the formyl-L-tryptophan-chymotrypsin complex, the residues on the AT-terminal side of lysine then form an antiparallel jS-structure with the enzyme similar to that proposed for y-chymostrypsin (1). There appear to be a number of favourable hydro-... 

They have been isolated from different mammalian organs and fluids—pancreas. parotid and submaxillary glands, intestinal wall kidney, urine, pancreatic juice, saliva and plasma. There are considerable differences in chemical properties among kallikreins of different origin. A multiplicity of kallikreins exists even within one organ of one species. 

Kininogenases are inhibited by numerous substances. In particular, the inhibition of kallikrein has been thoroughly studied since its discovery. One of the inhibitors, a polyvalent inhibitor of kallikrein and trypsin extracted from bovine lungs, was used with partial success in the treatment of experimental and clinical pathological conditions where activation of different proteolytic and esterolytic enzymes is assumed to play an important rdle in pancreatitis, peritonitis, the Schwartzmann phenomenon, spontaneous fibrinolysis, endotoxin shock, etc. 

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