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Protein in invertebrates

Kopf, G.S., Woolkalis, M.J., and Gerton, G.L. (1986). Evidence for a guanine nucleotide-binding regulatory protein in invertebrate and mammalian sperm. J. Biol. Chem. 267 7327-7331. [Pg.227]

The helices are represented by the regularly coiled sections of the ribbon diagram. Myohemerythrin is an oxygen-carrying protein in invertebrates. Sign in at www.thomsonedu.com/login to see an animated version of this figure. [Pg.92]

Z. Shen and M. Jacobs-Lorena, Evolution of chitin-binding proteins in invertebrates, J. Mol. EvoL, 48 (1999) 341-347. [Pg.354]

T. Suetake, S. Tsuda, S. Kawabata, K. Miura, S. Iwanaga, K. Hikichi, K. Nitta, and K. Kawano, Chitin-binding proteins in invertebrates and plants comprise a common chitin-bind-ing structural motif, J. Biol. Chem., 275 (2000) 17929-17932. [Pg.354]

Cyprid major protein is a larval storage protein necessary for successful metamorphosis. " Production of cyprid major protein was increased in the barnacle Balanus amphitrite following exposure to both nonylphenol and estradiol, suggesting that it may be a potential biomarker of estrogen exposure in invertebrates such as barnacles. " "... [Pg.59]

Water birds have not been shown to be directly affected by acidification. However, the prey of waterbirds may be of concern as these lower food-chain organisms may have elevated levels of toxic metals related to acidification of their habitat. Moreover, most water birds rely on some component of the aquatic food-chain for their high protein diet. Invertebrates that normally supply caJcium to egg-laying birds or their growing chicks are among the first to disappear as lakes acidify. As these food sources are reduced or eliminated due to acidification, bird habitat is reduced and reproductive rate of the birds is affected. The Common Loon is able to raise fewer chicks, or none at all, on acidic lakes where fish populations are reduced 37 and 5S). However, in some isolated cases, food supplies can be increased when competitive species are eliminated (e.g.. Common Goldeneye ducks can better exploit insects as food when competition from fish is eliminated). The collective influences of acidification are difficult to quantify on a specific area basis but for species that rely on a healthy aquatic ecosystem to breed, acidification remains a continuing threat in thousands of lakes across eastern North America 14). [Pg.56]

HA receptors are classified into 4 subtypes Hi, H2, H3, and H4 (Hill et al, 1997). All four HA receptor types are metabotropic receptors and belong to the superfamily of G-protein coupled receptors. Ionotropic HA receptors are found in invertebrates (Hardie, 1989 Gisselmann et al., 2002) but are absent from vertebrates (Haas Panula, 2003). Of the four HA receptors, only the Hi, H2, and H3 receptors are found in brain. The recently discovered H4 receptor is predominantly present on leukocytes and may have a critical role in the immune system (Nguyen et al., 2001 Bakker, 2004 Haas 8i Panula, 2003). [Pg.153]

Senozan, N. et al. (1981) Hemocyanin of the giant keyhold limpet, Megathura crenulata. In Invertebrate Oxygen Binding Proteins Structure, Active Sites, andFunction (J. Lamy, and J. Lamy, eds.), pp. 703-717. Dekker, New York. [Pg.1112]

Stecca, B., Southwood, C. M., Gragerov, A. et al. The evolution of lipophilin genes from invertebrates to tetrapods DM-20 cannot replace proteolipid protein in CNS myelin. /. Neurosci. 20,4002-4010, 2000. [Pg.70]

Co-expression of human tau with the fly homolog of GSK3-P resulted in accelerated neurodegeneration and the formation of tau-immunoreactive inclusions. In contrast to what has been described in FTDP-17 and mouse models of tauopathies, tau-induced neurodegeneration involved programmed cell death. Taken together, it appears that conformationally altered, nonfilamentous human tau protein is neurotoxic in invertebrates. [Pg.757]

Vertebrates contain several proteins that maintain the integrity of the blood plasma circulatory system. These contain domains that are specific to vertebrates (Gla, FN1, FN2) (Patthy, 1985), domains that are found in different contexts in invertebrates and/or protists (FBG, APPLE, KR) (Xu and Doolittle, 1990 Eschenbacher et al., 1993 Wilson et al., 1993) and a domain that is found in all cellular life (trypsin-like serine protease, Tryp SPc). The invertebrate versions of these domains, however, are found in molecular contexts that differ considerably from their vertebrate extracellular counterparts, indicating that although these nonenzy-... [Pg.230]

Robertson DHL, Marie AD, Veggerby C, Hurst JL, Beynon RJ (2001) Characteristics of ligand binding and release by major urinary proteins. In Marchlewska-Koj A, Lepri JJ, Muller-Schwarze D (eds) Chemical signals invertebrates IX. Cluver/Plenum, New York, p 169... [Pg.286]

Tropomyosin is a protein found in vertebrates and invertebrates, but only the protein from invertebrates has allergic properties. It is frequently found in sea foods, such as shrimps, crabs, American lobsters. Pacific flying squids, and also in some species of cockroaches (Blattela germanica, Periplaneta americand), moths, spiders, and house dust mites (Dermatophagoides pteronyssinus, Dermatophagoides farinae) (Witteman et ah, 1994). [Pg.117]

The amount of collagen varies from one species to another and from tissue to tissue within the same species. Collagen comprises as much as one third of the total protein in the vertebrate body and in certain invertebrates, such as sponges and echinoderms as well as corals186, collagen may account for an even larger proportion of the total protein of the organism. [Pg.72]

Hunt, S. Polysaccharide-protein complexes in invertebrates. London, New York Academic Press 1970... [Pg.135]

Respiratory pigments similar to the vertebrate haemoglobins have also been identified in many invertebrates. These vary from small proteins with two Fe-porphyrin units to large molecules containing up to 190 Fe-porphyrin units. Myoglobin, the 02 storage protein in muscle tissue, is also a small iron-protoporphyrin protein. The crystal structures of this and a number of other porphyrin proteins are now known (Chapter 20.2, Table 11). [Pg.982]


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