vicia angustifolia/proteinase

Koblingen er lagret på utklippstavlen

ArtiklerKliniske studierPatenter

Velg sorteringstype

6 resultater

Trypsin reactivity site of the Vicia angustifolia proteinase inhibitor.

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

Trypsin [EC 3.4.21.4] modified (reactive site cleaved) Vicia angustifolia proteinase inhibitor was prepared at pH 3 with a catalytic amount of trypsin and purified using columns of Sephadex G-50 and DEAE-Sephadex A-25. The modified inhibitor, which still retained antitryptic activity, lost its

Primary structure of Vicia angustifolia proteinase inhibitor.

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

The complete amino acid sequence (72 amino acid residues) of a double-headed proteinase inhibitor from seeds of Vicia angustifolia L. var. segetalis Koch has been determined and compared with those of other double-headed inhibitors of known structure. Sequencing was performed by conventional methods

Isolation and activities of the trypsin-modified Vicia angustifolia proteinase inhibitor lacking carboxyl-terminal hexapeptide.

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

The Vicia angustifolia proteinase inhibitor was incubated with p-toluenesulfonyl-L-phenylalanine chloromethyl ketone-trypsin (EC 3.4.21.4) and a main product was isolated. The purified product was different to the first trypsin-modified V. angustifolia inhibitor. The C-terminal residues of the new

Proteinase inhibitor from Vicia angustifolia L. var. segetalis Koch. Isolation, characterization, and chemical modification.

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

The amino acid sequence of a Bowman-Birk type proteinase inhibitor from faba beans (Vicia faba L.).

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

The amino acid sequence of a Bowman-Birk type proteinase inhibitor (FBI) from seeds of faba bean (Vicia faba L.) was determined by analysis of peptide fragments generated by reduction and S-carboxymethylation of enzymatically modified inhibitors, which were obtained from native FBI by limited

Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds.

Bare registrerte brukere kan oversette artikler

Logg inn Registrer deg

Trypsin inhibitors from winter pea seeds (c.v. Frilene) have been purified by ammonium sulfate precipitation, gel filtration, and anion and cation exchange chromatography and shown to consist of six protease inhibitors (PSTI I, II, III, IVa, IVb, and V). Their molecular weights were determined by

Bli med på
facebooksiden vår

Herbal & Natural Medicine

Den mest komplette databasen med medisinske urter støttet av vitenskap

Fungerer på 55 språk
Urtekurer støttet av vitenskap
Urtegjenkjenning etter bilde
Interaktivt GPS-kart - merk urter på stedet (kommer snart)
Les vitenskapelige publikasjoner relatert til søket ditt
Søk medisinske urter etter deres effekter
Organiser dine interesser og hold deg oppdatert med nyheter, kliniske studier og patenter

Skriv inn et symptom eller en sykdom og les om urter som kan hjelpe, skriv en urt og se sykdommer og symptomer den brukes mot.
* All informasjon er basert på publisert vitenskapelig forskning