scholarly journals Effect of the Plastein Reaction in Presence of Extrinsic Amino Acids on the Protective Activity of Casein Hydrolysate against Ethanol-Induced Damage in HHL-5 Cells

Foods ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 112
Author(s):  
Li-Ying Bo ◽  
Jia-Nan Pang ◽  
Chun-Li Song ◽  
Tie-Jing Li
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Treatment Time ◽  
Biological Activities ◽  
Casein Hydrolysate ◽  
Protective Activity ◽  
Potential Health ◽  
Plastein Reaction ◽  
Casein Hydrolysates

Casein hydrolysates (CH) were prepared using papain and modified by the plastein reaction (CH-P) in the presence of extrinsic phenylalanine (CH-P-Phe) or tryptophan (CH-P-Trp). The in vitro protective activity of CH and its modified products against ethanol-induced damage in HHL-5 cells was investigated. The results showed that the modification by the plastein reaction reduced the amino group content of CH. However, the modification by the plastein reaction in the presence of extrinsic amino acids could enhance the antioxidant, proliferative, cell cycle arresting, and anti-apoptosis activity of CH. Biological activities of CH and its modified products in the HHL-5 cells varied depending on the hydrolysate concentration (1, 2, and 3 mg/mL) and treatment time (24, 48, and 72 h). Generally, higher biological activities were found after cell treatment with CH or its modified products at concentration of 2 mg/mL for 48 h compared to other treatments. In addition, CH modified in the presence of tryptophan (CH-P-Trp) showed higher biological activity than that modified in the presence of phenylalanine (CH-P-Phe). Based on the obtained results, it can be concluded that casein hydrolysates with enhanced biological activity and potential health benefits can be produced by papain and the plastein reaction with the incorporation of extrinsic amino acids.

scholarly journals Translational and Structural Requirements of the Early Nodulin Gene enod40, a Short-Open Reading Frame-Containing RNA, for Elicitation of a Cell-Specific Growth Response in the Alfalfa Root Cortex

2001 ◽  
Vol 21 (1) ◽  
pp. 354-366 ◽  
Author(s):  
Carolina Sousa ◽  
Christina Johansson ◽  
Celine Charon ◽  
Hamid Manyani ◽  
Christof Sautter ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Rna Structure ◽  
Open Reading Frames ◽  
In Vitro Translation ◽  
Cortical Cells ◽  
Root Cortex ◽  
Reading Frame ◽  
Early Nodulin

ABSTRACT A diversity of mRNAs containing only short open reading frames (sORF-RNAs; encoding less than 30 amino acids) have been shown to be induced in growth and differentiation processes. The early nodulin geneenod40, coding for a 0.7-kb sORF-RNA, is expressed in the nodule primordium developing in the root cortex of leguminous plants after infection by symbiotic bacteria. Ballistic microtargeting of this gene into Medicago roots induced division of cortical cells. Translation of two sORFs (I and II, 13 and 27 amino acids, respectively) present in the conserved 5′ and 3′ regions ofenod40 was required for this biological activity. These sORFs may be translated in roots via a reinitiation mechanism. In vitro translation products starting from the ATG of sORF I were detectable by mutating enod40 to yield peptides larger than 38 amino acids. Deletion of a Medicago truncatula enod40 region between the sORFs, spanning a predicted RNA structure, did not affect their translation but resulted in significantly decreased biological activity. Our data reveal a complex regulation of enod40action, pointing to a role of sORF-encoded peptides and structured RNA signals in developmental processes involving sORF-RNAs.

Design, synthesis and biological activities of pyrrole-3-carboxamide derivatives as EZH2 (enhancer of zeste homologue 2) inhibitors and anticancer agents

2020 ◽  
Vol 44 (6) ◽  
pp. 2247-2255
Author(s):  
Qifan Zhou ◽  
Lina Jia ◽  
Fangyu Du ◽  
Xiaoyu Dong ◽  
Wanyu Sun ◽  
...  
Keyword(s):  
Biological Activity ◽  
Anticancer Agents ◽  
Biological Activities ◽  
Activity Assay ◽  
Design Synthesis ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Enhancer Of Zeste

A novel series of pyrrole-3-carboxamides targeting EZH2 have been designed and synthesized. The structure–activity relationships were summarized by combining with in vitro biological activity assay and docking results.

The Presence of Novel Amino Acids in the Cytoplasmic Domain of Stem Cell Factor Results in Hematopoietic Defects inSteel17H Mice

Blood ◽  
1999 ◽  
Vol 94 (6) ◽  
pp. 1915-1925 ◽  
Author(s):  
Reuben Kapur ◽  
Ryan Cooper ◽  
Xingli Xiao ◽  
Mitchell J. Weiss ◽  
Peter Donovan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bone Marrow ◽  
Biological Activity ◽  
Stem Cell ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Stem Cell Factor ◽  
Cytoplasmic Domain

Abstract Stem cell factor (SCF) is expressed as an integral membrane growth factor that may be differentially processed to produce predominantly soluble (S) (SCF248) or membrane-associated (MA) (SCF220) protein. A critical role for membrane presentation of SCF in the hematopoietic microenvironment (HM) has been suggested from the phenotype of the Steel-dickie(Sld) mice, which lack MA SCF, and by studies performed in our laboratory (and by others) using long-term bone marrow cultures and transgenic mice expressing different SCF isoforms.Steel17H (Sl17H) is an SCF mutant that demonstrates melanocyte defects and sterility in males but not in females. The Sl17H allele contains a intronic mutation resulting in the substitution of 36 amino acids (aa’s) in the SCF cytoplasmic domain with 28 novel aa’s. This mutation, which affects virtually the entire cytoplasmic domain of SCF, could be expected to alter membrane SCF presentation. To investigate this possibility, we examined the biochemical and biologic properties of the Sl17H-encoded protein and its impact in vivo and in vitro on hematopoiesis and on c-Kit signaling. We demonstrate that compound heterozygous Sl/Sl17H mice manifest multiple hematopoietic abnormalities in vivo, including red blood cell deficiency, bone marrow hypoplasia, and defective thymopoiesis. In vitro, both S and MA Sl17H isoforms of SCF exhibit reduced cell surface expression on stromal cells and diminished biological activity in comparison to wild-type (wt) SCF isoforms. These alterations in presentation and biological activity are associated with a significant reduction in the proliferation of an SCF-responsive erythroid progenitor cell line and in the activation of phosphatidylinositol 3-Kinase/Akt and mitogen-activated protein-Kinase signaling pathways. In vivo, transgene expression of the membrane-restricted (MR) (SCFX9/D3) SCF in Sl/Sl17H mutants results in a significant improvement in peripheral red blood cell counts in comparison toSl/Sl17H mice.

scholarly journals Biological activity of the red alga Laurencia brandenii

2011 ◽  
Vol 70 (1) ◽  
pp. 81-90 ◽  
Author(s):  
Aseer Manilal ◽  
Sugathan Sujith ◽  
Balu Sabarathnam ◽  
George Kiran ◽  
Joseph Selvin ◽  
...  
Keyword(s):  
Biological Activity ◽  
Biological Activities ◽  
Sitophilus Oryzae ◽  
Red Alga ◽  
Culture Collection ◽  
Gas Chromatography Mass Spectrometry ◽  
Human Pathogens ◽  
Active Fraction ◽  
Renewable Natural Resource

Biological activity of the red algaLaurencia brandeniiThe marine red algaLaurencia brandeniicollected from the southwest coast of India (Indian Ocean) was extracted and fractioned using column chromatography. The individual fractions were evaluatedin vitrovia antimicrobial activity against six species of Microbial Type Culture Collection and three species of clinical human pathogens, antipest activity onSitophilus oryzae, maggoticidal activity against 2ndinstar larvae ofSarcophagasp. and termiticidal activity againstMicrotermes obesi.It was found that the fraction eluted using petroleum ether:chloroform (6:4) exhibited broader biological activities. The phyco-constituents of the active fraction were identified by gas chromatography-mass spectrometry (GC-MS) analysis. The GC-MS profile of the active fraction revealed that the main constituent was octadecadienoic acid (49.75%) followed by n-hexadecanoic acid (14.24%), which might have a functional role in the biological activities. The overall activity profile envisages that these bioactive compounds fromL. brandeniicould be utilized as a renewable natural resource for the development of novel environmental-compatible formulations for the control of human pathogens, pests, termites and maggots.

scholarly journals Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

2013 ◽  
Vol 31 (No. 6) ◽  
pp. 559-567 ◽  
Author(s):  
Y. Zhang ◽  
X-H. Zhao
Keyword(s):  
Reaction Time ◽  
Casein Hydrolysate ◽  
Ace Inhibition ◽  
Water Medium ◽  
Kinetic Evaluation ◽  
Precipitation Inhibition ◽  
Calcium Chelation ◽  
Plastein Reaction ◽  
Zinc Chelation

Casein hydrolysate with in vitro ACE-inhibitory activity of 44.4% at 0.3 mg/ml was generated from casein by Alcalase and modified by the Alcalase-catalysed plastein reaction in an ethanol-water medium. Eight treated hydrolysates were prepared using the reaction time of 1-8 h under ethanol or substrate concentration, Alcalase addition and reaction temperature of 56.8% (v/v) or 56.8% (w/v), 8.4 kU/g peptides and 37.5&deg;C, respectively. Most of the treated hydrolysates showed enhanced ACE-inhibition compared to casein hydrolysate, and a reaction time of 4 h brought about the highest ACE-inhibition. All treated hydrolysates had lower zinc- or calcium-chelation but slightly higher iron(II)-chelation than casein hydrolysate, and a reaction time of 4 or 2 h could grant the treated hydrolysates the highest zinc- or calcium-chelation. Kinetic evaluation indicated that casein hydrolysate and two treated hydrolysates were competitive inhibitors to ACE. ACE-inhibition of these evaluated hydrolysates originated from themselves but was uncorrelated with their zinc-chelation, while their CaCO<sub>3</sub> precipitation inhibition was clearly correlated with their measured calcium-chelation (P &lt; 0.05).

scholarly journals Biological activities of recombinant chicken leptin C4S analog compared with unmodified leptins

2000 ◽  
Vol 279 (1) ◽  
pp. E116-E123 ◽  
Author(s):  
S. Dridi ◽  
N. Raver ◽  
E. E. Gussakovsky ◽  
M. Derouet ◽  
M. Picard ◽  
...  
Keyword(s):  
Biological Activity ◽  
Food Intake ◽  
Leptin Receptor ◽  
Biological Activities ◽  
Wild Type ◽  
Escherichia Coli Cells ◽  
Prokaryotic Expression Vector ◽  
Long Form

The chicken leptin sequence, in contrast to mammalian leptins, contains an unpaired Cys at position 3 of the original cDNA ( AF012727 ). The presence of an extra Cys may confer a different structure and affect the leptin's biological activity. To address this, we studied the effects of wild-type and mutated (C4S) chicken leptins in vitro and in vivo and compared them with mammalian leptin prepared from ovine leptin cDNA. The prokaryotic expression vector pMON, encoding full-size A(−1) chicken leptin ( AF012727 ), was mutated using a mutagenesis kit, yielding the C4S analog. Escherichia coli cells transformed with this vector overexpressed large amounts of chicken leptin C4S upon induction with nalidixic acid. The expressed protein, found in the inclusion bodies, was refolded and purified to homogeneity on a Q-Sepharose column, yielding three electrophoretically pure fractions, eluted from the column by 100, 125, and 150 mM NaCl, respectively. All three fractions showed a single band of the expected molecular mass (16 kDa) and were composed of >95% monomeric protein. Proper refolding was evidenced by comparing the circular dichroism spectrum of the analog with spectra of nonmutated chicken and ovine leptins. The biological activity of the C4S analog was evidenced by its ability to stimulate proliferation of leptin-sensitive BAF/3 cells transfected with a long form of human leptin receptor construct similar to its nonmutated counterpart, indicating that Cys4 plays no role in leptin activity. The in vitro activity of both wild-type and mutated chicken leptins was ∼10-fold lower than that of ovine leptin. After intravenous or intraperitoneal injections, C4S analog and the nonmutated chicken and ovine leptins all lowered the food intake of starved 9-day-old broiler or 5-wk-old layer male chickens by 11–34%. Monitoring food behavior revealed that the attenuated food intake resulted not from a decreased number of approaches to the feeders but from a decrease in the average time spent eating during each approach.

Antibacterial activity and in vitro cytotoxicity evaluation of alginate-AgNP fibers

2016 ◽  
Vol 87 (11) ◽  
pp. 1377-1386 ◽  
Author(s):  
Xihui Zhao ◽  
Qun Li ◽  
Xiaowen Li ◽  
Yanzhi Xia ◽  
Bing Wang ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Treatment Time ◽  
Biological Activities ◽  
In Vitro Cytotoxicity ◽  
Cell Counting ◽  
Logarithmic Phase ◽  
E Coli ◽  
Alginate Fibers ◽  
And Staphylococcus Aureus

Biopolymer nanocomposites containing metal nanoparticles have attracted much attention due to their excellent properties and broad applications. In this work, alginate fibers embedded with silver nanoparticles (AgNPs) were prepared. The as-obtained alginate-AgNP fibers exhibited antibacterial activity against both Gram microorganisms of model microbes Escherichia coli (Gram-negative) and Staphylococcus aureus (Gram-positive). A growth kinetic study with S. aureus and E. coli displayed the inhibition of bacterial growth at the logarithmic phase. The cytotoxic effect of the fibers in human cervical cancer (HeLa) cells was assessed by cell counting kit-8 (CCK-8) assay and flow cytometry. The as-prepared alginate-AgNP fibers, particularly with high amount and long treatment time, showed high cell-killing efficiency. These findings emphasize that such alginate-AgNP fibers with multifaceted biological activities are a promising material for applications in the textile or biomedical fields.

Phosphoramidate Derivatives of AZT as Inhibitors of HIV: Studies on the Carboxyl Terminus

1993 ◽  
Vol 4 (2) ◽  
pp. 97-101 ◽  
Author(s):  
C. McGuigan ◽  
R. N. Pathirana ◽  
S. S.-M. Choi ◽  
D. Kinchington ◽  
T. J. O'Connor
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Carboxyl Terminus ◽  
Amino Ester ◽  
Carboxy Terminus ◽  
Free Nucleotides ◽  
Derivatives Of ◽  
Anti Hiv ◽  
Ester Lead

Novel phosphoramidate derivatives of the anti-HIV nucleoside analogue AZT have been prepared by phosphorochloridate chemistry. These materials carry carboxy-protected, amino acids, and are designed to act as membrane-soluble prodrugs of the bio-active free nucleotides. In vitro evaluation revealed the compounds to have a pronounced, selective antiviral activity. In particular, variation in the carboxy terminus region is studied. For alkyl phosphates small changes in the structure of the amino ester lead to marked changes in biological activity. However, for analogous aryl phosphates there is little dependence on the structure of the ester. This suggests a different mechanism of action for these two categories of phosphate prodrug.

Biological characterization of charge isomers of human growth hormone

1988 ◽  
Vol 118 (1) ◽  
pp. 14-21 ◽  
Author(s):  
A. Skottner ◽  
A. Forsman ◽  
B. Skoog ◽  
J. L. Kostyo ◽  
C. M. Cameron ◽  
...  
Keyword(s):  
Biological Activity ◽  
Biological Activities ◽  
Human Growth ◽  
Proteolytic Processing ◽  
Biological Characterization ◽  
Growth Promoting ◽  
Rat Adipose Tissue ◽  
Insulin Like Activity

Abstract. Since deamidation of the human GH molecule may alter the manner and extent to which the hormone is cleaved by proteases, and since it has been repeatedly suggested that proteolytic processing is required for the expression of certain of the activities of GH, the present study was conducted to determine whether the biological activity profiles of more acidic forms of human GH are altered. Three charge isomers, GH-b, GH-c and GH-d, representing primarily deamidated forms, were isolated from a native human GH preparation (Crescormon®) in amounts adequate for characterization of their biological activities. All three were essentially equipotent in a radioimmunoassay for human GH. When assessed for growth-promoting activity in the hypophysectomized rat, the isomers were again equipotent with each other and with the GH preparation from which they were derived. The charge isomers also had significant in vitro insulin-like activity on isolated rat adipose tissue and diabetogenic activity in the ob/ob mouse. Thus, the biological activity profiles of these charge isomers of human GH do not differ greatly from one another.

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