Database of Biologically Active Proteins and Peptides

2012 ◽  
pp. 331-374 ◽  
Author(s):  
Bartłomiej Dziuba ◽  
Piotr Minkiewicz ◽  
Małgorzata Darewicz
Keyword(s):  
Biologically Active ◽  
Proteins And Peptides

Properties and Biotechnological Application of mutant Derivatives of Mini-intein PRP8 from Penicillium chrysogenum with Improved Control of C-terminal Processing

2019 ◽  
Vol 35 (6) ◽  
pp. 91-101
Author(s):  
F.A. Klebanov ◽  
S.E. Cheperegin ◽  
D.G. Kozlov
Keyword(s):  
Penicillium Chrysogenum ◽  
Protein Denaturation ◽  
Biologically Active ◽  
Cultivation Temperature ◽  
Target Proteins ◽  
E Coli ◽  
Complete Inactivation ◽  
Target Molecules ◽  
Proteins And Peptides

Mutant variants of mini-intein PRP8 from Penicillium chrysogenum (Int4b) with improved control of C-terminal processing were characterized. The presented variants can serve as a basis for self-removed polypeptide tags capable of carrying an affine label and allowing to optimize the process of obtaining target proteins and peptides in E. coli cells. They allow to synthesize target molecules in the composition of soluble and insoluble hybrid proteins (fusions), provide their afnne purification, autocatalytic processing and obtaining mature target products. The presented variants have a number of features in comparison with the known prototypes. In particular the mutant mini-intein Int4bPRO, containing the L93P mutation, has temperature-dependent properties. At cultivation temperature below 30 °C it allows the production of target molecules as part of soluble fusions, but after increasing of cultivation temperature to 37 °C it directs the most of synthesized fusions into insoluble intracellular aggregates. The transition of Int4bPRO into insoluble form is accompanied by complete inactivation of C-terminal processing. Further application of standard protein denaturation-renaturation procedures enable efficiently reactivate Int4bPRO and to carry out processing of its fusions in vitro. Two other variants, Int4b56 and Int4b36, containing a point mutation T62N or combination of mutations D144N and L146T respectively, have a reduced rate of C-terminal processing. Their use in E. coli cells allows to optimize the biosynthesis of biologically active target proteins and peptides in the composition of soluble fusions, suitable for afnne purification and subsequent intein-dependent processing without the use of protein denaturation-renaturation procedures. intein, fusion, processing, processing rate, gelonin The work was supported within the framework of the State Assignment no. 595-00003-19 PR.

Comparison of immunomodulatory properties of purified lactoferrin, lactoperoxidase and β-casein in sheep

1998 ◽  
Vol 65 (4) ◽  
pp. 697-701 ◽  
Author(s):  
CHUN W. WONG ◽  
DENNIS L. WATSON ◽  
GEOFFREY O. REGESTER ◽  
GEOFFREY W. SMITHERS
Keyword(s):  
Biomedical Applications ◽  
Bovine Milk ◽  
Milk Proteins ◽  
Biologically Active ◽  
Immunological Effects ◽  
Bovine Milk Proteins ◽  
Proteins And Peptides

Bovine milk contains a variety of proteins and peptides that are biologically active (Ogra & Ogra, 1978; Duncan & McArthur, 1981; Newby et al. 1982; Juto, 1985; Stoeck et al. 1989; Mincheva-Nilsson et al. 1990; Watson, 1990; Barta et al. 1991; Politis et al. 1991; Fiat et al. 1993). Our laboratory has a long-term interest in some purified milk proteins, particularly lactoferrin (LF), lactoperoxidase (LP) and β-casein (β-CN), which have been shown to be immunologically significant. Some of our recent studies on these bovine milk proteins, particularly β-CN, indicated that their in vitro immunological effects did not always parallel their in vivo activities (Wong et al. 1996a, b; 1997a, b). This study was designed to investigate and compare the capacity of these purified bovine milk proteins to modulate a range of components that are vital to in vivo immune responses in sheep, with a view to providing further information on their potential in biomedical applications. To achieve this objective, a sensitive lymphatic cannulation model was employed that allows in vivo immune components and their functions to be measured in lymph collected under physiological conditions.

scholarly journals Isolation and Analytical Characterization of Local Malaysian Leech Saliva

1970 ◽  
Vol 12 (4) ◽  
Author(s):  
Mohamed Alaama ◽  
Manar AlNajjar ◽  
Abdualrahman Abdualkader ◽  
Abbas Mohammad ◽  
And Ahmed Merzouk
Keyword(s):  
Gel Electrophoresis ◽  
Extraction Method ◽  
Biologically Active ◽  
Protein Database ◽  
Molecular Weights ◽  
Rp Hplc ◽  
Bradford Assay ◽  
High Concentrations ◽  
Proteins And Peptides

Leech saliva contains biologically active compounds that are mainly proteins and peptides. In this study a modified and smooth extraction method of saliva was used without leeches' scarification. UV and Bradford Assay protein methods showed that the saliva extract contains high concentrations of proteins. RP-HPLC chromatogram revealed that more than 30 different peaks were observed in leech saliva extract. Gel electrophoresis revealed the existence of proteins and peptides with different molecular weights. The gel showed up to 25 different bands. Comparison of gel electrophoresis data with protein database revealed the closeness of four molecular weights to known proteins from Hirudinaria leech family. Other proteins detected by gel electrophoresis may be related to completely new biologically active proteins and peptides in the saliva extract or to a modification (isoforms) of the existing ones or finally to a mixture of both.ABSTRAK: Air liur pacat secara biologinya mengandungi sebahagian besar campuran aktif protein dan peptida. Dalam kajian ini, kaedah pengestrakan air liur pacat yang telah diubah suai digunakan tanpa perlu membunuh pacat. Kaedah protein Cerakin UV dan Bradford menunjukkan air liur pacat yang diekstrak mengandungi konsentrasi protein yang tinggi. Kromatogram RP-HPLC memperlihatkan lebih daripada 30 puncak berbeza diperolehi semasa air liur pacat diekstrak. Gel elektroforesis memperlihatkan kewujudan protein dan peptida dengan berat molekul yang berbeza. Gel menunjukkan hingga 25 jalur yang berbeza. Perbandingan data menggunakan gel elektroforesis seiring dengan pangkalan data protein memperlihatkan persamaan empat berat molekul, dengan protein yang yang dikenali daripada keluarga pacat Hirudinaria. Jenis protein lain yang dikesan dengan menggunakan gel elektrofosis mungkin juga berkait secara biologinya dengan protein dan peptida aktif yang baru, dalam ekstrak air liur atau pengubahsuaian (beberapa jenis yang berbeza daripada protein yang sama) daripada yang sedia ada ataupun gabungan kedua-duanya.KEY WORDS : leech saliva; RP-HPLC; gel electrophoresis.

scholarly journals Immuno-suppressive lymphocyte factors. I. Purification of inhibitor of DNA synthesis to homogeneity.

1979 ◽  
Vol 150 (3) ◽  
pp. 622-632 ◽  
Author(s):  
B V Jegasothy ◽  
D R Battles
Keyword(s):  
Dna Synthesis ◽  
T Lymphocyte ◽  
Gel Electrophoresis ◽  
Free Amino ◽  
Biologically Active ◽  
Gel Chromatography ◽  
Amino Groups ◽  
Very High ◽  
Tetrameric Form ◽  
Proteins And Peptides

Inhibitor of DNA synthesis (IDS) is a T-lymphocyte factor, whose role in immunnoregulation might be to nonspecifically suppress the immune system especially in situations where very high, prolonged tolerogenic doses of antigens are present. We have purified IDS-contained supernates of stimulated lymphocytes to homogeneity, through isoelectric focusing and Sephadex gel chromatography. IDS has an isoelectric point of 2.73-2.75 and in its monomeric form has a mol wt of 20,000 but exists in the supernate usually as an aggregated tetrameric form. Di- and trimeric forms are also seen. All forms are biologically active. Purity was confirmed by SDS gel electrophoresis and the binding of dansyl chloride to terminal or free amino groups of proteins and peptides. We have, further confirmed that pure IDS is not cytotoxic and is probably a glycoprotein whose activity depends on an intact carbohydrate moiety.

Modification of Fibroin Film with A Chimera Fibroin Fragment for Improvement of Cell Adhesion

1998 ◽  
Vol 530 ◽  
Author(s):  
Yasushi Tamada
Keyword(s):  
Phase Transition ◽  
Cell Adhesion ◽  
Silk Fibroin ◽  
Biological Molecules ◽  
Biologically Active ◽  
Random Coil ◽  
Structural Protein ◽  
Transition Mechanism ◽  
Regulation Functions ◽  
Proteins And Peptides

AbstractSilk fibroin is a naturally occurring structural protein with good mechanical properties used in a variety of forms, such as powder, fiber, film, and gel. Although silk fibroin is potentially suitable for use in tissue engineering, it lacks cell regulation functions such as cell adhesion, growth, metabolism, and differentiation. The immobilization of biologically active molecules such as proteins and peptides has been reported as promising in controlling cell behavior. Silk fibroin's phase transition is characterized by a conformational change of protein from a random coil to a beta sheet. During phase transition, biological molecules can be stably entrapped in silk fibroin without the use of chemicals. We designed a novel immobilization using this phase transition mechanism with a chimera fibroin fragment. The chimera fibroin fragment was constructed by linking a bioactive peptide to fibroin fragments including crystal regions. In the first study, a synthetic oligonucleotide encoding Arg-Gly-Asp peptide which promotes cell adhesion, was fused to the fibroin fragment gene through inframe gene fusion, and the chimera fibroin (RGD-fibroin) gene was expressed by E.coli. This paper discusses RGD-fibroin construction, and the results of cell adhesion on fibroin films containing RGD-fibroin.

scholarly journals Controlled Release of Protein from Viable Lactococcus lactis Cells

2010 ◽  
Vol 76 (9) ◽  
pp. 3026-3031 ◽  
Author(s):  
Régis Stentz ◽  
Roy J. Bongaerts ◽  
A. Patrick Gunning ◽  
Mike Gasson ◽  
Claire Shearman
Keyword(s):  
Cell Viability ◽  
Lactococcus Lactis ◽  
Active Form ◽  
Biologically Active ◽  
Bacterial Proteins ◽  
Novel Approach ◽  
Optimized Conditions ◽  
The Impact ◽  
Extracellular Environment ◽  
Proteins And Peptides

ABSTRACT Overexpression of the lactococcal CsiA protein affects the cell wall integrity of growing cells and leads to leakage of intracellular material. This property was optimized and exploited for the targeted release of biologically active compounds into the extracellular environment, thereby providing a new delivery system for bacterial proteins and peptides. The effects of different levels of CsiA expression on the leakage of endogenous lactate dehydrogenase and nucleic acids were measured and related to the impact of CsiA expression on Lactococcus lactis cell viability and growth. A leakage phenotype was obtained from cells expressing both recombinant and nonrecombinant forms of CsiA. As proof of principle, we demonstrated that CsiA promotes the efficient release of the heterologous Listeria bacteriophage endolysin LM4 in its active form. Under optimized conditions, native and heterologous active-molecule release is possible without affecting cell viability. The ability of CsiA to release intracellular material by controlled lysis without the requirement for an external lytic agent provides a technology for the control of both the extent of lysis and its timing. Taken together, these results demonstrate the potential of this novel approach for applications including product recovery in industrial fermentations, food processing, and medical therapy.

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