Category: Proteins
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Keratan sulfate (KS) aka keratosulfate
Not to be confused with Keratin. Keratan sulfate (KS), also called keratosulfate, is any of several sulfated glycosaminoglycans (structural carbohydrates) that have been found especially in the cornea, cartilage, and bone. It is also synthesized in the central nervous system where it participates both in development and in the glial scar formation following an injury. Keratan sulfates are large, highly hydrated molecules which in joints can act as a cushion to…
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Perivitellins are egg proteins found in the perivitelline fluid of many gastropods
Perivitellins are multifunctional complexes providing the developing embryo with nutrition, protection from the environment, and defense against predators. Despite the central role perivitellins play in reproduction and development, there is little information about their role in gastropod Molluscs. Most studies of perivitellins have been performed in eggs of Ampullaridae, a family of freshwater snails (Caenogastropoda), notably the Pomacea genus, mostly…
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Scalarin carries and stabilizes carotenoid pigments
Scalarin (PsSC) is the most abundant perivitellin of the perivitelline fluid from Pomacea scalaris eggs. This glyco-lipo-caroteno protein is an approx. 380 kDa multimer combining multiple copies of six different 24-35 kDa subunits. As part of the petivitelline fluid, PsSC is probably playing a role as a nutrient source for the developing embryo in Pomacea scalaris eggs. As its orthologous ovorubin and PmPV1, this protein carries and stabilizes carotenoid pigments. As…
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Pomacea maculata perivitellin-1 (PmPV1) is a glyco-lipo-caroteno protein
Pomacea maculata perivitellin-1 (PmPV1) is the most abundant perivitellin found in the perivitelline fluid from Pomacea maculata snail eggs. This glyco-lipo-caroteno protein is an approx. 294 kDa multimer of a combination of multiple copies of six different ~30 kDa subunits. PmPV1 account >60% of the total proteins found in the Pomacea maculata eggs. PmPV1 is an orthologous of ovorubin and scalarin, sharing most of the structural features with the former protein…
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Ovorubin
Ovorubin (PcOvo or PcPV1) is the most abundant perivitellin (>60 % total protein) of the perivitelline fluid from Pomacea canaliculata snail eggs. This glyco-lipo-caroteno protein complex is a approx. 300 kDa multimer of a combination of multiple copies of six different ~30 kDa subunits. Together with the other perivitellins from Pomacea canaliculata eggs, ovorubin serves a nutrient source for developing embryos, notably to the intermediate and late stages. Moreover, after hatching,…
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Clusterin (apolipoprotein J)
Clusterin (apolipoprotein J) is a 75-80 kDa disulfide-linked heterodimeric protein associated with the clearance of cellular debris and apoptosis. In humans, clusterin is encoded by the CLU gene on chromosome 8. CLU is a molecular chaperone responsible for aiding protein folding of secreted proteins, and its three isoforms have been differentially implicated in pro- or antiapoptotic processes. Through this function, CLU is involved in many diseases related to oxidative stress, including neurodegenerative diseases, cancers, inflammatory diseases, and aging. Structure The CLU gene contains…
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The Membrane Attack Complex/Perforin (MACPF) superfamily aka MACPF/CDC superfamily
See also: Complement membrane attack complex The Membrane Attack Complex/Perforin (MACPF) superfamily, sometimes referred to as the MACPF/CDC superfamily, is named after a domain that is common to the membrane attack complex (MAC) proteins of the complement system (C6, C7, C8α, C8β and C9) and perforin (PF). Members of this protein family are pore-forming toxins (PFTs). In eukaryotes, MACPF proteins play a role in immunity and development. Archetypal members of the family…
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Complement receptor type 1 (CR1)
Complement receptor type 1 (CR1) also known as C3b/C4b receptor or CD35 (cluster of differentiation 35) is a protein that in humans is encoded by the CR1 gene. This gene is a member of the regulators of complement activation (RCA) family and is located in the ‘cluster RCA’ region of chromosome 1. The gene encodes a monomeric single-pass type I membrane glycoprotein found on erythrocytes, leukocytes, glomerular podocytes, hyalocytes, and splenic follicular dendritic…
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Three-finger proteins and three-finger toxins
Three-finger proteins or three-finger protein domains (3FP or TFPD) are a protein superfamily consisting of small, roughly 60-80 amino acid residue protein domains with a common tertiary structure: three beta strand loops extended from a hydrophobic core stabilized by disulfide bonds. The family is named for the outstretched “fingers” of the three loops. Members of the family have no enzymatic activity, but are capable of forming protein-protein interactions with high specificity and affinity. The founding members of the…
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Effect of biotin deficiency on embryonic development in the domestic fowl (1944) with reference and cited by articles
The approximate biotin requirements of breeding hens have been established and the embryos examined for gross pathological symptoms and the approximate age at death are recorded. Cravens, W.W., W., & Sebesta, M.A. (1944). Effect of biotin deficiency on embryonic development in the domestic fowl. The Anatomical Record, 90. Reference articles Effect of Biotin on Reproduction in…
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Biotin
BIOTIN Biotin is involved in a wide range of metabolic processes in humans and in other organisms, primarily related to the utilization of fats, carbohydrates, and amino acids. The name biotin, borrowed from the German Biotin, derives from the Ancient Greek βίοτος (bíotos; ‘life’) and the suffix “-in” (used in chemistry to indicate ‘forming’). AKA…
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Avidin is a tetrameric biotin-binding protein produced in the oviducts of birds, reptiles, amphibians
Dimeric members of the avidin family are also found in some bacteria. In chicken egg white, avidin makes up approximately 0.05% of total protein (approximately 1800 μg per egg). The tetrameric protein contains four identical subunits (homotetramer), each of which can bind to biotin (Vitamin B7, vitamin H) with a high degree of affinity and specificity. The dissociation constant of the avidin-biotin complex…
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The NACHT domain consists of seven distinct conserved motifs, including the ATP/GTPase specific P-loop, the Mg2+-binding site (Walker A and B motifs, respectively) and five more specific motifs
The NACHT domain is an evolutionarily conserved protein domain. This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription. Its name reflects some of the proteins that contain it: NAIP (NLP family apoptosis inhibitor protein), CIITA (that is, C2TA or MHC class II transcription activator), HET-E (incompatibility locus protein from Podospora anserina) and TEP1 (that is, TP1 or telomerase-associated protein). The NACHT domain contains 300 to 400 amino acids. It is…
