Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook.

The amino acid sequence of the cysteine proteinase CC-III from the latex of the subtropical species Carica candamarcensis Hook has been determined with the exception of seven residues (pos. 180-186). It was deduced from the sequence analysis of the whole chain and peptides obtained by tryptic, chymotryptic, peptic and thermolysinolytic hydrolysis.

Isolation and preliminary characterization of the cysteine-proteinases from the latex of Carica candamarcensis Hook.

The cysteine-proteinase chymopapain from Carica papaya L. is used for chemonucleolysis of damaged human intervertebral spinal discs. The purification of this enzyme is difficult.

The thiol proteinases from the latex of Carica papaya L. IV. Proteolytic specificities of chymopapain and papaya proteinase omega determined by digestion of alpha-globin chains.

The proteolytic specificities of chymopapain and papaya proteinase omega were investigated by using the alpha-chains of manatee and mole haemoglobin, whose primary structures are known, as substrates. The resulting peptides from each enzymatic cleavage were isolated by gel filtration on Sephadex G-25, followed by reversed-phase HPLC of the separated peaks and, in some cases, further purified by preparative thin-layer electrophoresis. The purified peptides were then identified on the basis of their amino-acid composition.

The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain.

The amino-acid sequence of chymopapain is presented. It was isolated from the latex of the fruits from the tropical species Carica papaya L. and is, besides papain and papaya proteinase omega, the third thiol proteinase from this source.

The influence of experimental conditions on the spectrin-hemoglobin interaction.

Human spectrin, when isolated, purified and stored in such conditions that preserve its tetrameric form, is able to associate with human hemoglobin as it is clearly shown by gel filtration. However, this hemoglobin-spectrin association does not seem to have a significant effect on hemoglobin oxygenation as indicated by equilibrium and rapid kinetics measurements.

Separation and characterization of four enzyme forms of beta-galactosidase from Saccharomyces lactis.

beta-Galactosidase from Saccharomyces lactis has been purified to serve as a model for the kinetic behavior of human lactase in adult lactase deficiency. Enzymes from both species are neutral and follow Michaelis-Menten kinetics. beta-Galactosidase of S.

The thiol proteinases from the latex of Carica papaya L. I. Fractionation, purification and preliminary characterization.

Three thiol proteinases, namely papain, chymopapain and proteinase omega were purified to homogeneity from the latex of Carica papaya L. During the purification procedure, the thiol function of the cysteinyl residues were protected either as mixed disulfides with cysteamine or 2-thiopyridone or as S-sulphenylthiosulfate derivative or after blocking with p-chloromercuribenzoic acid. In marked contrast with earlier publications, chymopapain also was found to be a monothiol proteinase as papain and proteinase omega.

The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega.

The complete primary structure of the proteinase omega isolated from the latex of the Carica papaya fruits is given. The polypeptide chain contains 216 amino-acid residues, the alignment of which was deduced from sequence analyses of the native enzyme, the tryptic, chymotryptic, peptic and thermolysinolytic peptides and facilitated due to the considerable degree of homology with papain and actinidin. The location of the three disulfide bridges could be established with the help of peptic and thermolysinolytic fragments.

Caiman crocodylus hemoglobin. Complete primary structures of alpha and beta chains; phylogenic and regulatory aspects.

In some reptiles, the hemoglobin oxygen affinity is lowered by CO2 and not by the usual phosphate cofactors. To understand the molecular mechanism of this regulation, Caiman crocodylus hemoglobin's primary structure has been determined. The alignment of the 141 residues of the alpha chain as well as the 146 of the beta chain were obtained by classical method of sequence analysis and are compared with some mammalian, avian, amphibian, and fish hemoglobin chains.

Reoxidation of reduced hen egg white lysozyme fragment 1-123.

The reactivation of reduced lysozyme, whose 6 COOH-terminal amino acid including cysteine 127 were cut off, was studied. The results show that the disulfide bridge I-VIII as well as the COOH-terminal hexapeptide do not play a decisive role in the acquisition of the native 3-dimensional structure of the enzyme.

The primary sequence of chicken myoglobin (Gallus gallus).

After enzymatic digestion of chicken myoglobin by trypsin, chymotrypsin or thermolysin, the separation of peptides was performed by column chromatography on various ion exchange resins. Each peptide was purified by high-voltage paper electrophoresis or by chromatography either on paper or on ion-exchange resin, and its complete amino acid sequence was then determined by the combined dansyl-Edman procedure and by endopeptidase digestions. The whole globin was submitted to automatic Edman degradation using the Beckman sequencer.