Nothing Special   »   [go: up one dir, main page]

Hatano et al., 1995 - Google Patents

Primary structure, sequence‐specific 1H‐NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem

Hatano et al., 1995

View PDF
Document ID
12734760001503705945
Author
Hatano K
Kojima M
Tanokura M
Takahashi K
Publication year
Publication venue
European journal of biochemistry

External Links

Snippet

One of the bromelain inhibitors, isoinhibitor VI (BI‐VI), was purified from pineapple stem powder and its complete amino acid sequence was determined by conventional protein sequencing. These results revealed that the protein consists of an 11‐residue light chain …
Continue reading at febs.onlinelibrary.wiley.com (PDF) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors
    • C07K14/8107Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/811Serine protease (E.C. 3.4.21) inhibitors
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/43504Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K1/00General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/06General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents
    • C07K1/061General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using protecting groups
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K7/00Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04Linear peptides containing only normal peptide links
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K5/00Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00Medicinal preparations containing peptides
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K8/00Cosmetic or similar toilet preparations
    • A61K8/18Cosmetic or similar toilet preparations characterised by the composition

Similar Documents

Publication Publication Date Title
Ghiso et al. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C).
Strobl et al. Determination of the three-dimensional structure of the bifunctional. alpha.-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy
Saxena et al. Protein proteinase inhibitors from avian egg whites
US6645934B1 (en) Peptide with radio protective effect
Griffith et al. Reactive site peptide structural similarity between heparin cofactor II and antithrombin III.
Kobayashi et al. The cystine‐stabilized α‐helix: A common structural motif of ion‐channel blocking neurotoxic peptides
Méndez et al. Primary structure of ω‐hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell‐free systems
Thiele et al. Substance K and substance P as possible endogenous substrates of angiotensin converting enzyme in the brain
Antuch et al. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata
Odani et al. Proteinase Inhibators from a Mimosoideae Legume
Wu et al. A structural and functional analogue of a Bowman–Birk-type protease inhibitor from Odorrana schmackeri
Takahashi et al. Cathepsins B and H from porcine spleen. Purification, polypeptide chain arrangements, and carbohydrate content.
Bonnet et al. Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide
Hatano et al. Primary structure, sequence‐specific 1H‐NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem
Adjadj et al. Solution Structure of Lqh‐8/6, a Toxin‐Like Peptide from a Scorpion Venom: Structural Heterogeneity Induced by Proline Cis/Trans Isomerization
Schultes et al. Complete amino‐acid sequence of glyceraldehyde‐3‐phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
US5151509A (en) Gene encoding serine protease inhibitor
Towatari et al. Amino acid sequence of rat liver cathepsin L
LENAČIČ et al. Characterization and structure of pineapple stem inhibitor of cysteine proteinases
D'AVINO et al. Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta: 2. Amino acid sequence of the α chain of Hb 1
Widmer et al. The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence‐specific 1H‐NMR assignments
Highberger et al. Comparative studies on the amino acid sequence of the α2-CB2 peptides from chick and rat skin collagens
Suyemitsu et al. The exogastrula-inducing peptides in embryos of the sea urchin, Anthocidaris crassispina—isolation and determination of the primary structure
Weber et al. The isolation of tubulin and actin from mouse 3T3 cells transformed by simian virus 40 (SV3T3 cells), an established cell line growing in culture
Martin et al. Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases