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phytolacca americana/protease

הקישור נשמר בלוח
מאמריםניסויים קלינייםפטנטים
10 תוצאות

Purification and properties of a protease from the sarcocarp of bead tree fruit.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
A protease was purified from bead tree fruit (Melia azedarach L. var. japonica Makino) in four steps, including HPLC gel-filtration. The M(r) of the enzyme, named melain, was estimated to be 25,000 on SDS-PAGE and on HPLC gel filtration. Melain contained a carbohydrate moiety. Using casein as a

Isolation and characterisation of a cysteine protease (phytolacain G), from Phytolacca americana roots.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Protein extracts obtained from dried and fresh roots of Phytolacca americana L. (Phytolaccaceae) were examined in order to identify and characterise individual proteins. The extracts were compared with a commercial pokeweed mitogen standard using SDS polyacrylamide gel electrophoresis (SDS-PAGE). A

Amino acid sequence and some properties of phytolacain R, a cysteine protease from full-growth fruits of pokeweed, Phytolacca americana.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
A cysteine protease, phytolacain R from full-growth greenish fruits of pokeweed, Phytolacca americana L, was purified to electrophoretic homogeneity by a simple purification procedure employing CM-Sepharose ion-exchange chromatography. The enzyme was present in low content in the young fruits about

Amino acid sequence and some properties of phytolacain G, a cysteine protease from growing fruit of pokeweed, Phytolacca americana.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
A protease, phytolacain G, has been found to appear on CM-Sepharose ion-exchange chromatography of greenish small-size fruits of pokeweed, Phytolacca americana L, from ca. 2 weeks after flowering, and increases during fruit enlargement. Reddish ripe fruit of the pokeweed contained both phytolacain G

Comparison of phytolacain G, a cysteine protease from fruit of Phytolacca americana, with phytolacain R.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The enzymatic properties of phytolacain G, a protease isolated from green fruit of pokeweed, were compared with those of phytolacain R, a protease obtained from ripe fruit. The optimum pH of phytolacain G was 7.5-8.0 at 37 degrees C using casein as the substrate. The enzyme was strongly inhibited by

Comparison of phytolacain R, a cysteine protease from Phytolacca americana, with papain.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Nine sites of oxidized insulin B-chain were cleaved by phytolacain R, isolated from pokeweed, after 20 hr of hydrolysis. Five cleavage sites resembled those of papain. Substrate specificity of phytolacain R was similar to that of papain, preferring hydrophobic P2 residues. The activities of fibrin

Amino acid sequences of two ferredoxins from pokeweed, Phytolacca americana.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The amino acid sequences of two ferredoxins isolated from pokeweed, Phytolacca americana, were determined. Tryptic peptides of maleyl-carboxymethyl-ferredoxin I and carboxymethyl-ferredoxin II were prepared and analyzed. The large peptides were further digested with staphylococcal protease and

A non-toxic pokeweed antiviral protein mutant inhibits pathogen infection via a novel salicylic acid-independent pathway.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Pokeweed antiviral protein (PAP), a ribosome-inactivating protein isolated from Phytolacca americana, is characterized by its ability to depurinate the sarcin/ricin (S/R) loop of the large rRNA of prokaryotic and eukaryotic ribosomes. In this study, we present evidence that PAP is associated with

Complete amino acid sequence of chitinase-A from leaves of pokeweed (Phytolacca americana).

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The complete amino acid sequence of pokeweed leaf chitinase-A was determined. First all 11 tryptic peptides from the reduced and S-carboxymethylated form of the enzyme were sequenced. Then the same form of the enzyme was cleaved with cyanogen bromide, giving three fragments. The fragments were
Ribosome-inactivating proteins are N-glycosidases that remove a specific adenine from the sarcin/ricin loop of the large rRNA, thus arresting protein synthesis at the translocation step. In the present study, a novel type I ribosome-inactivating protein, termed PAP-H, was purified from Agrobacterium
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