Natural rubber latex (NRL) allergy is caused by the extractable latex proteins in dipped rubber products. It is a major concern for the consumers who are sensitive to the allergenic extractable proteins (EP) in products such as NRL gloves. Objective of this research was to develop an economical method to reduce the EP in finished dipped NRL products. In order to reduce the EP levels, two natura...

Various properties of crystalline papain have been under investigation in this laboratory for several years in attempts to understand the specificity, mode of action, and other aspects of the behavior of this enzyme (1). Inasmuch as papain must be in its native state to retain its enzymic activity, a knowledge of the role of the amino acid side chains in maintaining conformation is essential. T...

Contamination of food products by spoilage and pathogenic microorganisms during post process handling is one of the major causes for food spoilage and food borne illnesses. The present green sustainable approach describes the covalent immobilization of papain to LDPE (low density polyethylene), HDPE (high density polyethylene), LLDPE (linear low density polyethylene) and PCL (polycaprolactam) w...

Z-Phe-Ala-glyoxal (where Z is benzyloxycarbonyl) has been synthesized and shown to be a competitive inhibitor of papain with a K(i)=3.30+/-0.25 nM. (13)C-NMR has been used to show that in aqueous media, Z-Phe-[2-(13)C]Ala-glyoxal gives signals at 207.7 p.p.m. and 96.3 p.p.m. showing that both the alpha-keto carbon and its hydrate are present. When this inhibitor is bound to papain a single sign...

The ability of papain to split esters of the type hydrolyzed by trypsin has been reported from this laboratory (1) and has also been independently observed by other workers (2) at about the same time. The esters studied here were the methyl esters of cY-N-benzoylarginine and its nitro derivatives. It was observed that the presence of a nitro group on the benzene ring of the ester altered consid...

AN ultracentrifuge study of the action of papain on egg albumin was made in this laboratory [Svedberg & Eriksson, 1933; 1934], but with the centrifugal forces and methods of measurement then available it was not possible to separate effectively the digestion products obtained. It was therefore thought advisable to use the improved apparatus now in the laboratory to extend these observations. As...

Protein crystals isolated from potato tubers were found to consist of a proteinase inhibitor active against the cysteine proteinases papain, chymopapain, and ficin. The molecular weight as determined by gel filtration at pH 4.3 or by gel electrophoresis in the presence of dodecylsulfate was 80 kilodaltons. When the inhibitor was evaluated at pH 8.4 in a linear concentration (4-30% polyacrylamid...

Attempts to cocrystallize the cysteine protease papain derived from the latex of Carica papaya with an inhibitor of cysteine proteases (ICP) from Trypanosoma brucei were unsuccessful. However, crystals of papain that diffracted to higher resolution, 1.5 A, than other crystals of this archetypal cysteine protease were obtained, so the analysis was continued. Surprisingly, the substrate-binding c...

Two hairpin-loop domains in cystatin family proteinase inhibitors form an interface surface region that slots into the active site cleft of papain-like cysteine proteinases, and determine binding affinity. The slot region surface architecture of the soybean cysteine proteinase inhibitor (soyacystatin N, scN) was engineered using techniques of in vitro molecular evolution to define residues that...

Fluorescence studies have been performed on the interaction of papain with active-site-directed inhibitors of the type mansyl-(Gly)n-Phe-glycinal, where n = 0, 1, 2. It has been found that whereas the mansyl [6-(N-methylantilino)-2-naphthalene sulfonyl] fluorescence of mansyl-Phe-glycinal is greatly enhanced, that of the two longer mansyl compounds is not, although all three are equally effecti...