Antifreeze Proteins
Retinol-Binding Proteins, Cellular
Antifreeze Proteins, Type I
Antifreeze Proteins, Type III
Retinol-Binding Proteins
Flounder
Bone Morphogenetic Protein Receptors, Type I
Antifreeze Proteins, Type IV
Antifreeze Proteins, Type II
Vitamin A
Fishes
Marinomonas
Antarctic Regions
Glycoproteins
Bone Morphogenetic Protein Receptors, Type II
Flatfishes
Salmoniformes
Secale cereale
Beetles
Amino Acid Sequence
Molecular Sequence Data
Lysosomal-Associated Membrane Protein 2
Daucus carota
Models, Molecular
Crystallization
Smad1 Protein
Protein Conformation
Protein Structure, Secondary
Perciformes
Neutron Diffraction
Smad6 Protein
Gadiformes
Base Sequence
Circular Dichroism
Smad5 Protein
Isolation and characterization of type I antifreeze proteins from Atlantic snailfish (Liparis atlanticus) and dusky snailfish (Liparis gibbus). (1/16)
Antifreeze proteins (AFPs) were isolated from the blood plasma of Atlantic snailfish Liparis atlanticus and dusky snailfish Liparis gibbus, which belong to the Teleost family Cyclopteridae, a close relative of sculpins. Using a combination of gel filtration chromatography and reversed-phase HPLC, proteins were purified to individual peaks. Atlantic snailfish plasma contained two different proteins (MW=9344, 9415) while dusky snailfish plasma contained five protein isoforms (MW=9514-9814), as determined by mass spectrometry. Further characterization revealed that these proteins are rich in alanine (>50 mol%), and have alpha-helical secondary structure that can undergo reversible thermal denaturation. Thermal hysteresis activities of these proteins were similar to each other but lower than the major type I AFPs from winter flounder. Results of this study have indicated that although the AFPs from snailfish are significantly larger than previously described type I AFPs, they share enough characteristics to be classified in this group. (+info)Structure of type I antifreeze protein and mutants in supercooled water. (2/16)
Many organisms are able to survive subzero temperatures at which bodily fluids would normally be expected to freeze. These organisms have adapted to these lower temperatures by synthesizing antifreeze proteins (AFPs), capable of binding to ice, which make further growth of ice energetically unfavorable. To date, the structures of five AFPs have been determined, and they show considerable sequence and structural diversity. The type I AFP reveals a single 37-residue alpha-helical structure. We have studied the behavior of wild-type type I AFP and two "inactive" mutants (Ala17Leu and Thr13Ser/Thr24Ser) in normal and supercooled solutions of H(2)O and deuterium oxide (D(2)O) to see if the structure at temperatures below the equilibrium freezing point is different from the structure observed at above freezing temperatures. Analysis of 1D (1)H- and (13)C-NMR spectra illustrate that all three proteins remain folded as the temperature is lowered and even seem to become more alpha-helical as evidenced by (13)C(alpha)-NMR chemical shift changes. Furthermore, (13)C-T(2) NMR relaxation measurements demonstrate that the rotational correlation times of all three proteins behave in a predictable manner under all temperatures and conditions studied. These data have important implications for the structure of the AFP bound to ice as well as the mechanisms for ice-binding and protein oligomerization. (+info)A mechanism for stabilization of membranes at low temperatures by an antifreeze protein. (3/16)
Polar fish, cold hardy plants, and overwintering insects produce antifreeze proteins (AFPs), which lower the freezing point of solutions noncolligatively and inhibit ice crystal growth. Fish AFPs have been shown to stabilize membranes and cells in vitro during hypothermic storage, probably by interacting with the plasma membrane, but the mechanism of this stabilization has not been clear. We show here that during chilling to nonfreezing temperatures the alpha-helical AFP type I from polar fish inhibits leakage across model membranes containing an unsaturated chloroplast galactolipid. The mechanism involves binding of the AFP to the bilayer, which increases the phase transition temperature of the membranes and alters the molecular packing of the acyl chains. We suggest that this change in acyl chain packing results in the reduced membrane permeability. The data suggest a hydrophobic interaction between the peptide and the bilayer. Further, we suggest that the expression of AFP type I in transgenic plants may be significant for thermal adaptation of chilling-sensitive plants. (+info)Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein. (4/16)
The solution structure of a synthetic mutant type I antifreeze protein (AFP I) was determined in aqueous solution at pH 7.0 using nuclear magnetic resonance (NMR) spectroscopy. The mutations comprised the replacement of the four Thr residues by Val and the introduction of two additional Lys-Glu salt bridges. The antifreeze activity of this mutant peptide, VVVV2KE, has been previously shown to be similar to that of the wild type protein, HPLC6 (defined here as TTTT). The solution structure reveals an alphahelix bent in the same direction as the more bent conformer of the published crystal structure of TTTT, while the side chain chi1 rotamers of VVVV2KE are similar to those of the straighter conformer in the crystal of TTTT. The Val side chains of VVVV2KE assume the same orientations as the Thr side chains of TTTT, confirming the conservative nature of this mutation. The combined data suggest that AFP I undergoes an equilibrium between straight and bent helices in solution, combined with independent equilibria between different side chain rotamers for some of the amino acid residues. The present study presents the first complete sequence-specific resonance assignments and the first complete solution structure determination by NMR of any AFP I protein. (+info)Freezing of a fish antifreeze protein results in amyloid fibril formation. (5/16)
Amyloid is associated with a number of diseases including Alzheimer's, Huntington's, Parkinson's, and the spongiform encephalopathies. Amyloid fibrils have been formed in vitro from both disease and nondisease related proteins, but the latter requires extremes of pH, heat, or the presence of a chaotropic agent. We show, using fluorescence spectroscopy, electron microscopy, and solid-state NMR spectroscopy, that the alpha-helical type I antifreeze protein from the winter flounder forms amyloid fibrils at pH 4 and 7 upon freezing and thawing. Our results demonstrate that the freezing of some proteins may accelerate the formation of amyloid fibrils. (+info)The effect of hydrophobic analogues of the type I winter flounder antifreeze protein on lipid bilayers. (6/16)
The effect of four synthetic analogues of the 37-residue winter flounder type I antifreeze protein (AFP), which contain four Val, Ala or Ile residues in place of Thr residues at positions 2, 13, 24 and 37 and two additional salt bridges, on the binary lipid system prepared from a 1:1 mixture of the highly unsaturated DGDG and saturated DMPC has been determined using FTIR spectroscopy. In contrast to the natural protein, which increases the thermotropic phase transition, the Thr, Val and Ala analogues decreased the thermotropic phase transitions of the liposomes by 2.2 degrees Celsius, 3.4 degrees Celsius and 2.4 degrees Celsius, while the Ile analogue had no effect on the transition. Experiments performed using perdeuterated DMPC showed that the Ala and Thr peptides interacted preferentially with the DGDG in the lipid mixture, while the Val peptide showed no preference for either lipid. The results are consistent with interactions involving the hydrophobic face of type I AFPs and model bilayers, i.e. the same face of the protein that is responsible for antifreeze properties. The different effects correlate with the helicity of the peptides and suggest that the solution conformation of the peptides has a significant role in determining the effects of the peptides on thermotropic membrane phase transitions. (+info)Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices. (7/16)
The winter flounder (Pseudopleuronectes americanus) produces short, monomeric alpha-helical antifreeze proteins (type I AFP), which adsorb to and inhibit the growth of ice crystals. These proteins alone are not sufficiently active to protect this fish against freezing at -1.9 degrees C, the freezing point of seawater. We have recently isolated a hyperactive antifreeze protein from the plasma of the flounder with activity 10-100-fold higher than type I AFP. It is comparable in activity to the AFPs produced by insects, and is capable of conferring freeze resistance to the flounder. This novel AFP has a molecular mass of 16,683 Da and a remarkable amino acid composition that is >60% alanine. CD spectra indicate that the protein is almost entirely alpha-helical at 4 degrees C but partially denatures at 20 degrees C, resulting in a species with a moderately reduced helix content that is stable at up to 50 degrees C. This transformation correlates with irreversible loss of activity. Analytical ultracentrifugation (sedimentation velocity and equilibrium) indicates that the predominant species in solution is dimeric (molecular weight, 32,275). Size-exclusion chromatography reveals a 2-fold higher apparent molecular weight suggesting that this molecule has an unusually large Stokes radius. The axial ratio of the dimer calculated from the sedimentation velocity data is 18:1, confirming that this protein has an extraordinarily long, rod-like structure, consistent with a novel dimeric alpha-helical arrangement. The structural model that best fits these data is one in which the approximately 195 amino acids of each monomer form one approximately 290-A long alpha-helix and associate via a unique dimerization motif that is distinct from that of the leucine zipper and any other coiled-coil. (+info)Type I antifreeze proteins expressed in snailfish skin are identical to their plasma counterparts. (8/16)
Type I antifreeze proteins (AFPs) are usually small, Ala-rich alpha-helical polypeptides found in right-eyed flounders and certain species of sculpin. These proteins are divided into two distinct subclasses, liver type and skin type, which are encoded by separate gene families. Blood plasma from Atlantic (Liparis atlanticus) and dusky (Liparis gibbus) snailfish contain type I AFPs that are significantly larger than all previously described type I AFPs. In this study, full-length cDNA clones that encode snailfish type I AFPs expressed in skin tissues were generated using a combination of library screening and PCR-based methods. The skin clones, which lack both signal and pro-sequences, produce proteins that are identical to circulating plasma AFPs. Although all fish examined consistently express antifreeze mRNA in skin tissue, there is extreme individual variation in liver expression - an unusual phenomenon that has never been reported previously. Furthermore, genomic Southern blot analysis revealed that snailfish AFPs are products of multigene families that consist of up to 10 gene copies per genome. The 113-residue snailfish AFPs do not contain any obvious amino acid repeats or continuous hydrophobic face which typify the structure of most other type I AFPs. These structural differences might have implications for their ice-crystal binding properties. These results are the first to demonstrate a dual liver/skin role of identical type I AFP expression which may represent an evolutionary intermediate prior to divergence into distinct gene families. (+info)The exact cause of myositis ossificans is not fully understood, but it is thought to be related to an abnormal repair process within the muscle tissue. The condition can be diagnosed through a combination of physical examination, imaging studies such as X-rays or MRIs, and biopsy.
Treatment for myositis ossificans usually focuses on relieving pain and improving mobility. This may include rest, physical therapy, anti-inflammatory medications, and in some cases, surgery to remove the abnormal bone growth. The condition can take several months to resolve, and in rare cases, it may recur.
Myositis ossificans is a relatively rare condition, but it can have a significant impact on an individual's quality of life, particularly if left untreated. It is important for healthcare providers to be aware of this condition and its symptoms in order to provide accurate diagnosis and appropriate treatment.
Sources:
* American Academy of Orthopaedic Surgeons. (2019). Myositis Ossificans. Retrieved from
* MedlinePlus. (2020). Myositis ossificans. Retrieved from
* UW Health. (n.d.). Myositis Ossificans. Retrieved from
Antifreeze protein
Sclerotinia borealis
RiAFP
Neofunctionalization
Crystal
Genetically modified fish
Ocean pout
Snailfish
Polyproline helix
Genetically modified animal
Psychrophile
Dendroides canadensis
Xylomannan
Flavobacterium xanthum
Antifreeze
Bald notothen
Notothenia neglecta
List of examples of convergent evolution
Pseudomonas syringae
Beetle
Nysius wekiuicola
Index of protein-related articles
Hibernaculum (zoology)
Notothenia angustata
Homaxinella balfourensis
Hair ice
Cryobiology
Cryothenia
Eurytherm
Plant
Hibernation
Polyethylene glycol
Thermoregulation
Fish physiology
Artedidraconidae
Vitrification
Preservative
Mitochondrial optic neuropathies
Notothenia microlepidota
Pyrolysis
Southern Ocean
Silanization of silicon and mica
Moss lawn
Cockroach
Toothpaste
Optic neuropathy
List of dog diseases
Cold hardening
Arthrobacter agilis
Rainbow smelt
Antifreeze Proteins, Type II | Harvard Catalyst Profiles | Harvard Catalyst
SCOPe 2.01: Structural Classification of Proteins - extended
Biomarkers Search
MeSH Browser
Regulation of a cold inducible antifreeze protein in soil bacterium Pseudomonas putida GR12-2
MeSH Browser
DeCS - New terms
Apolipoproteínas/análise
Publications - Voets Research Group
Aquaculture Research Group | Page 2 | - CCMAR
NDF-RT Code NDF-RT Name
Zhejiang University, China, Chemistry
RESEARCH - Chirality at the Nanoscale
Volume 225 Issue Suppl 1 | Journal of Experimental Biology | The Company of Biologists
Snailfish - Encyclopedia Information
CryoLetters 33 (2), 2012
NEW (2001) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; revised 9/6/2000
Keith Price Bibliography Bibtex Entry (URL http://dx.doi.org/10.1007/978-3-662-44415-3 10 TYPE CONFERENCE PAGES 93-102 MONTH...
Antifreeze Market Size, Share, Trends and Industry Outlook by 2030
DeCS - Termos Novos
View source - 2010.igem.org
Osmolality Tests: MedlinePlus Medical Test
Frontiers | Variations on primary metabolites of the carrageenan-producing red algae Sarcopeltis skottsbergii from Chile and...
PlantPromoterDB promoter information of AT5G15960
TERM
Evolution of the human brain: when bigger is better
Browsing DSpace : HUSCAP
Brooks, Bernard 2020 - Office of NIH History and Stetten Museum
Organisms And Environment Test Online Questions & Answers Mcqs
August | 2022 | FrogHeart
Subclass6
- A subclass of ANTIFREEZE PROTEINS that have a cystine-rich globular structure of approximately 14 kD. (harvard.edu)
- A subclass of ANTIFREEZE PROTEINS that contain four amphipathic alpha-helices folded into an antiparallel helix bundle. (nih.gov)
- use ANTIFREEZE PROTEINS (NM) 1980-2000 BX - Antifreeze Glycoproteins MH - Antifreeze Proteins, Type I UI - D021322 MN - D12.776.53.100 MS - A subclass of ANTIFREEZE PROTEINS that are 3-5 kD in size and contain a single alanine-rich amphipathic alpha-helix. (nih.gov)
- HN - 2001 MH - Antifreeze Proteins, Type II UI - D021341 MN - D12.776.53.200 MS - A subclass of ANTIFREEZE PROTEINS that have a cystine-rich globular structure of approximately 14 kD. (nih.gov)
- HN - 2001 MH - Antifreeze Proteins, Type III UI - D021343 MN - D12.776.53.350 MS - A subclass of ANTIFREEZE PROTEINS that are globular, 6.5 kD in size and contain compact beta-sheet structures. (nih.gov)
- HN - 2001 MH - Antifreeze Proteins, Type IV UI - D021302 MN - D12.776.53.500 MS - A subclass of ANTIFREEZE PROTEINS that contain four amphathic alpha-helices folded into an antiparallel helix bundle. (nih.gov)
20011
- HN - 2001 BX - Vaccines, Anthrax MH - Antifreeze Proteins UI - D021301 MN - D12.776.53 MS - Proteins that bind to ice and modify the growth of ice crystals. (nih.gov)
Peptides2
- use ANTIFREEZE PROTEINS (NM) 1997-2000 MH - Antimicrobial Cationic Peptides UI - D023181 MN - D12.644.350 MN - D24.611.600 MS - Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. (nih.gov)
- use ANTIMICROBIAL CATIONIC PEPTIDES (NM) to search MICROBICIDAL CATIONIC PROTEINS 1981-2000 BX - Microbicidal Cationic Proteins FX - Blood Bactericidal Activity MH - Antiretroviral Therapy, Highly Active UI - D023241 MN - E2.319.310.75 MS - Drug regimens, for patients with HIV INFECTIONS, that aggressively supress HIV replication. (nih.gov)
Inducible1
- cold and ABA inducible protein kin1, possibly functions as an anti-freeze protein. (gifu-u.ac.jp)
Binds1
- The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. (nih.gov)
Toggle1
- Team Aberdeen_Scotland:]] The AyeSwitch: a translationally regulated genetic toggle switch in yeast=== A novel genetic toggle switch regulated at the translational level was engineered in yeast that allowed the mutually exclusive expression of either green or cyan fluorescent protein. (igem.org)
Specificity1
- Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. (nih.gov)
Gene6
- Transcriptional regulation of this protein was investigated by studying the DNA upstream of the antifreeze gene. (uwaterloo.ca)
- The genomes of both the Yap hadal Snailfish and Mariana hadal Snailfish have been found to contain an abundance of the fmo3 gene, which produces the trimethylamine N-oxide (TMAO) protein stabilizer. (webot.org)
- However, protein activity of GUS fused to the promoter of this gene is inhibited by cold treatment, suggesting an inhibition of the protein by increased transcript level. (gifu-u.ac.jp)
- Required for the transcriptional activation of the flounder liver-type antifreeze protein gene. (nih.gov)
- Mutations in this gene lead to spinal muscle atrophy with respiratory distress type 1. (nih.gov)
- Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 16.8 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
MeSH1
- Antifreeze Proteins, Type II" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Lipid2
- BACKGROUND: Evidence suggests that proteins related to lipid metabolism, such as apolipoproteins, play an important role in the maintenance of normal vision. (bvsalud.org)
- The gelatinous layer has a high water and low protein, lipid and carbohydrate content, therefore it can provide growth with low metabolic cost. (webot.org)
Urine1
- You may need a serum osmolality or urine osmolality test if you have symptoms of a fluid imbalance, diabetes insipidus, or certain types of poisoning. (medlineplus.gov)
Enzymes2
- Further, their genome includes increased amounts of genes encoding enzymes for beta oxidation and transport proteins, thereby increasing membrane fluidity. (webot.org)
- The tight regulation of [H+] at this low concentration is crucial for normal cellular activities because H+ at higher concentrations can bind strongly to negatively charged proteins, including enzymes, and impair their function. (medscape.com)
Bacterium1
- In the soil bacterium Pseudomonas putida GR12-2, expression of antifreeze protein AfpA was previously observed to be regulated by cold induction at 5 degrees Celsius. (uwaterloo.ca)
Species1
- Several studies reported that gametophytes and tetrasporophytes of Gigartinaceae produce different carrageenan types, as observed in Sarcopeltis species although they have isomorphic haploid and diploid phases. (frontiersin.org)
Molecular2
- Molecular docking simulations results show that the contact surface area and binding energy of proteins to CDS-PMo12@PVP1 NPs are smaller than the CDS-PMo12@PVP0 NPs. (bvsalud.org)
- The agency cites examples such as ice-binding proteins - found in fish, bacteria, and plants - that affect ice formation at the molecular level. (sandboxx.us)
Molecules2
- These properties could be leveraged as part of the ICE program to develop persistent anti-icing coatings for surfaces and even produce specialized small molecules that work synergistically with biodegradable antifreeze proteins. (sandboxx.us)
- Chemist studies protein molecules that make animals glow in the dark. (nih.gov)
Regulation3
- To better understand how this antifreeze protein helps with low temperature survival, I investigated AfpA regulation at multiple levels. (uwaterloo.ca)
- Using cell cytometry (FACS) and fluorimetry, we demonstrated in yeast the successful expression and translational regulation of a fusion of mRNA binding protein and fluorescent protein. (igem.org)
- Proteins help with pH regulation within cells. (webmd.com)
Substances2
- Plasma contains substances including blood cells and certain proteins. (medlineplus.gov)
- In addition, a variety of substances such as fuel, water, antifreeze, dust, and various combustion products such as polycyclic aromatic hydrocarbons (PAHs), metals, and metallic oxides accumulate in the oil. (cdc.gov)
Similarity2
Inhibition1
- This protein was identified to have ice recrystallization inhibition activity, a putative ice binding site and is likely secreted by a type I secretion system. (uwaterloo.ca)
Metabolism1
- Teodósio R, Aragão C, Conceição LEC, Dias J, Engrola S . Amino Acid Metabolism in Gilthead Seabream Is Affected by the Dietary Protein to Energy Ratios . (ualg.pt)
Drugs1
- Research may play a significant role in developing the next generation of drugs to treat a type of cancer. (nih.gov)
Genome1
- Additionally, perhaps due to lack of light in the deep sea, the Yap genome includes fewer copies of crystallin genes, which encode proteins that sense light and assist in focused vision, in comparison to other teleosts. (webot.org)
Growth3
- These proteins assist in survival below 0 degrees Celsius by minimizing extracellular ice crystal growth. (uwaterloo.ca)
- Aragão C, Gonçalves ATeresa, Costas B, Azeredo R, Xavier MJoão, Engrola S . Alternative Proteins for Fish Diets: Implications beyond Growth . (ualg.pt)
- All types of organisms are capable of reproduction, growth and development, maintenance, and some degree of response to stimuli. (testadvisor.in)
Regulate2
- Herein, we introduce a family of structurally homologous PMo12-based NPs (CDS-PMo12@PVPx(x = 0 ~ 1) NPs) capping diverse content of zwitterionic polymer poly (N-vinylpyrrolidone) (PVP) to regulate the protein corona formation on PMo12-based NPs. (bvsalud.org)
- Hemoglobin, the main protein inside your red blood cells, helps regulate pH there. (webmd.com)
Production5
- In cold inhabiting bacteria, a commonly used strategy to combat freezing stress is the production of antifreeze proteins. (uwaterloo.ca)
- Increasing vehicle production, especially SUV & light truck segment and recent growing trend in trucks & buses segment in countries such as India are the key reasons driving the demand for OE market for antifreeze. (marketsandmarkets.com)
- Thus, the sales and production of passenger cars is increasing and leading to increased demand for engine coolant and antifreeze. (marketsandmarkets.com)
- The North American region leads the antifreeze market for the automotive industry, owing to the higher production and demand for large engine capacity vehicles in this region such as extended cabs. (marketsandmarkets.com)
- Additionally, the automotive industry of North America is one of the most advanced across the globe with substantial investments in R&D activities, infrastructure, and new production facilities driving the overall automotive antifreeze market. (marketsandmarkets.com)
Specific1
- DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. (nih.gov)
Activity3
- With a temperature dependent activity, these proteins are regulated by changes in ambient temperature. (uwaterloo.ca)
- Hagit Kun and Y. Mastai 'Activity of Short Segments of Type I Antifreeze Protein. (mastai-lab.com)
- Relationships between cold hardiness, and ice nucleating activity, glycerol and protein contents in the hemolymph of caterpillars, Aporia crataegi L. (cryoletters.org)
Size1
- These factors have contributed to the higher market size of automotive antifreeze in this region. (marketsandmarkets.com)
Transport3
- revised 9/6/2000) TOTAL DESCRIPTORS = 184 MH - Active Transport, Cell Nucleus UI - D021581 MN - G6.535.166.310.100 MN - G6.535.166.700.100 MS - Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE. (nih.gov)
- This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. (nih.gov)
- Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (nih.gov)
Chemical2
Higher3
- Also, glycols used for antifreeze are manufactured from crude oil filtration, which may lead to a higher demand for fossil fuels such as crude oil and can have a negative impact on the environment. (marketsandmarkets.com)
- Also, LCVs in North America have a higher antifreeze requirement, as compared to other regions. (marketsandmarkets.com)
- Primary metabolites of S. antarctica varied according to the life-history phases: non-fertile specimens presented higher phycobiliprotein concentrations, tetrasporophytes presented higher chlorophyll a concentrations, and cystocarpic specimens presented higher concentrations of proteins, polysaccharides and floridean starch. (frontiersin.org)
Small1
- While several members of the apolipoprotein family are abundant in human aqueous humor (AH), their study remains difficult due to the AH's small volume, low protein concentration, and the invasive nature of sample collection. (bvsalud.org)
Year2
- This graph shows the total number of publications written about "Antifreeze Proteins, Type II" by people in Harvard Catalyst Profiles by year, and whether "Antifreeze Proteins, Type II" was a major or minor topic of these publication. (harvard.edu)
- Growing vehicles in operation and increased miles travelled per year is estimated to drive the demand for antifreeze in aftermarket segment. (marketsandmarkets.com)
Include1
- These include excess salt intake , kidney disease , heart disease , and some types of poisoning . (medlineplus.gov)
Nature1
- Antifreeze base fluids are toxic in nature. (marketsandmarkets.com)
Addition1
- In addition, 76 differentially adsorption proteins are identified between CDS-PMo12@PVP0 and CDS-PMo12@PVP1 NPs, in which apolipoprotein is up-regulated in CDS-PMo12@PVP1 NPs. (bvsalud.org)
Prevent1
- One type is caused by defective anti-oncogenes, which prevent oncogenes from causing cancer. (preterhuman.net)
Factors1
- Then, we tested the hypothesis if the variation on primary metabolites (pigments, proteins and carbohydrates) are related to the life history phases of Sarcopeltis antarctica and Sarcopeltis skottsbergii , and/or are influenced by abiotic factors. (frontiersin.org)
Plasma1
- The number of plasma protein groups adsorption on CDS-PMo12@PVP1 NPs, compared to CDS-PMo12@PVP0 NPs, decreases from 372 to 271. (bvsalud.org)
Properties1
- 2. HEALTH EFFECTS contaminants in the oil increases with use and varies depending on the type of fuel used and the mechanical properties of the engine. (cdc.gov)