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sweet potato/protease
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Seite 1 von 53 Ergebnisse
Sweet potato cysteine proteases SPAE and SPCP2 participate in sporamin degradation during storage root sprouting.
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Sweet potato sporamins are trypsin inhibitors and exhibit strong resistance to digestion by pepsin, trypsin and chymotrypsin. In addition, they constitute the major storage proteins in the sweet potato and, after degradation, provide nitrogen as a nutrient for seedling regrowth in sprouting storage
Sweet potato SPAP1 is a typical aspartic protease and participates in ethephon-mediated leaf senescence.
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Plant aspartic proteases are generally divided into three categories: typical, nucellin-like, and atypical aspartic proteases based on their gene and protein structures. In this report, a full-length cDNA SPAP1 was cloned from sweet potato leaves, which contained 1515 nucleotides (504 amino acids)
Molecular cloning and characterization of a granulin-containing cysteine protease SPCP3 from sweet potato (Ipomoea batatas) senescent leaves.
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Granulins are a family of evolutionarily ancient proteins that are involved in regulating cell growth and division in animals. In this report a full-length cDNA, SPCP3, was isolated from senescent leaves of sweet potato (Ipomoea batatas). SPCP3 contains 1389 nucleotides (462 amino acids) in its open
Protease production with sweet potato residue by solid state fermentation.
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The sweet potato residue being at the initial moisture content 50-58%, initial pH 3.5-4.3, supplemented with rice bran, and minerals, and incubated at 20-26 degrees C for 5 days was the optimal conditions for protease production with Aspergillus niger NTU-AM-1 by solid state fermentation. Protease
Strawberry Mottle Virus (Family Secoviridae, Order Picornavirales) Encodes a Novel Glutamic Protease To Process the RNA2 Polyprotein at Two Cleavage Sites.
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Strawberry mottle virus (SMoV) belongs to the family Secoviridae (order Picornavirales) and has a bipartite genome with each RNA encoding one polyprotein. All characterized secovirids encode a single protease related to the picornavirus 3C protease. The SMoV 3C-like protease was
A novel serine protease from strawberry (Fragaria ananassa): Purification and biochemical characterization.
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In this study, a protease enzyme was purified from strawberry by using Sepharose-4B-l-tyrosine-p-amino benzoic acid affinity chromatography. The molecular weight of pure protease was determined 65.8 kDa by SDS-PAGE. The single band observed on the gel showed that the enzyme had a single polypeptide
Expression of sweet potato cysteine protease SPCP2 altered developmental characteristics and stress responses in transgenic Arabidopsis plants.
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In this report a full-length cDNA, SPCP2, which encoded a putative papain-like cysteine protease was isolated from senescent leaves of sweet potato (Ipomoea batatas). SPCP2 contained 1101 nucleotides (366 amino acids) in its open reading frame, and exhibited high amino acid sequence identities (ca.
Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus.
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Strawberry mottle virus (SMoV, family Secoviridae, order Picornavirales) is one of several viruses found in association with strawberry decline disease in Eastern Canada. The SMoV genome consists of two positive-sense single-stranded RNAs, each encoding one large polyprotein. The RNA1 polyprotein
Corrigendum: Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus.
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[This corrects the article on p. 745 in vol. 8, PMID: 28496438.].
Analysis of complete genomic sequences of isolates of the Sweet potato feathery mottle virus strains C and EA: molecular evidence for two distinct potyvirus species and two P1 protein domains.
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The complete nucleotide sequence of the isolate C1 of Sweet potato feathery mottle virus (SPFMV) strain C and the 5' region of several other strains were determined and analyzed together with the sequences of isolates representing the EA, RC and O strains. This provided molecular evidence for the
A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.
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Glutaredoxins (Grx) play an important role in reduction of protein glutathione mixed disulphides. An IbGrx cDNA (561 bp, EF362614) encoding a putative dithiol Grx was cloned from sweet potato (Ipomoea batatas [L.] Lam). The deduced amino acid sequence is conserved among the reported dithiol Grx,
Partial cleavage of sweet potato feathery mottle virus coat protein subunit by an enzyme in extracts of infected symptomless leaves.
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The coat protein of particles of sweet potato feathery mottle potyvirus (SPFMV) extracted from Ipomoea spp. migrated in SDS-PAGE mainly as bands of M(r) 38,000 (38K), 36K, 32K, 30K. Trypsin treatment of the particles resulted in the appearance of only one 30K polypeptide. The inclusion of protease
Production and In Vitro Gastrointestinal Digestion of Antioxidant Peptides from Enzymatic Hydrolysates of Sweet Potato Protein Affected by Pretreatment.
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Effects of ultrasonication, boiling, steaming, microwaving and autoclaving pretreatments on the production of sweet potato protein hydrolysates (SPPH) by single and combined Alcalase (ALC) and Protease (PRO) were investigated, as well as antioxidant activities of SPPH subjected to in vitro
Anti-breast-Cancer Activity Exerted by β-Sitosterol-d-glucoside from Sweet Potato via Upregulation of MicroRNA-10a and via the PI3K-Akt Signaling Pathway.
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Breast cancer (BC) is a prominent source of cancer mortality in women throughout the world. β-Sitosterol-d-glucoside (β-SDG), a newly isolated phytosterol from sweet potato, possibly displays potent anticancer activity. However, the probable anticancer mechanisms involved are still unclear. This
Alpha-glucan phosphorylase from sweet potato: isolation and properties of the partially degraded enzyme.
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Alpha-Glucan phosphorylase (EC 2.4.1.1.) was purified from sweet potato roots. Apparently homogeneous preparations obtained are partially degraded products from phosphorylase, as judged from the results of molecular weight determination, NH-2-termini analysis and pyridoxal-5'-P assay. Phosphorylase
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