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Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a rela­tively few species. A comparative examination of the inhibition of trypsin, chymo- trypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemo­lymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors exa­mined fall into two groups: low molecular mass proteins (below 10 kDa) related to Kunitz type inhibitors, and proteins of about 45 kDa which belong to the serpin superfamily of serine proteinase inhibitors. This minireview describes the properties, characteristics and possible biological significance of selected inhibitors.
The rats fed for two generations F₀/F₁ with 80%wheat or rye diet, were kiled in the age of 3 mouths of F₁ and blood serum was taken. The activity of cholinesterase, ceruloplasmine, basic phosphatase and Kunitz antitrypsic activity were measured. Blood serum protein, protein electrophoretic fractions (albumins to globulina ratio) and cholesterol levels were estimated. No difference of ceruloplasmine, basic phosphatase activities and total cholesterol levels in rats fed rye or wheat was noted, which proves no changes in the internal liver transport. However the singnificant (p=0.001) difference in choliesterase activity and total protein level in blood serum showes inhibition of protein synthesis in the liver.
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The antioxidant capacity as free radicals of 1,1 diphenyl-2-picryhydrazyl (DPPH) scavenger of egg white protein hydrolysate was investigated. Egg white protein precipitate obtained as a by-product in cystatin and lysozyme isolation was hydrolysed with bovine trypsin and then separated by means of RP-HPLC. Of ten fractions collected only no. 2 (0.195 μmol Trolox /mg) and no. 5 (0.186 μmol Trolox /mg) displayed a considerable free radicalscavenging capacity. The rechromatography of these fractions yielded four products of raised antioxidant activity: no. 2E (obtained from fraction no. 2) and no. 5E, 5F, 5H (obtained from fraction no. 5) which amounted to 0.482 μmol Trolox /mg and 0.584, 1.375, 1.200 μmol Trolox /mg, respectively.
Two serine proteinase inhibitors (ELTII and ELT1II) have been isolated from mature seeds of Echinocystis lobata by ammonium sulfate fractionation, methanol preci­pitation, ion exchange chromatography, affinity chromatography on immobilized anhydrotrypsin and HPLC. ELTI I and ELTI II consist of 33 and 29 amino-acid residues, respectively. The primary structures of these inhibitors are as follows: ELTI I KEEQRVCPRILMRCKRDSDCLAQCTCQQSGFCG ELTI II RVCPRILMRCKRDSDCLAQCTCQQSGFCG The inhibitors show sequence similarity with the squash inhibitor family. ELTI I differs from ELTI II only by the presence of the NH2-terminal tetrapeptide Lys- -Glu-Glu-Gln. The association constants (Ka) of F.LTI I and ELTI II with bovine-trypsin were determined to be 6.6 x 1010 M -1 and 3.1 x 1011 M -1, whereas the association constants of these inhibitors with cathepsin G were 1.2 x 107 M -1 and 1.1 x 107 M -1, respectively.
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