Results 21 to 30 of about 19,494 (217)
Structure of arthropod hemocyanin [PDF]
, 1986 Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map ...
Henk J. Bak +23 more
core +1 more source
Rondonin: antimicrobial properties and mechanism of action
FEBS Open Bio, 2021 Infectious diseases are among the major causes of death in the human population. A wide variety of organisms produce antimicrobial peptides (AMPs) as part of their first line of defense.
Katie C. T. Riciluca +5 more
doaj +1 more source
The Oxidation of Hemocyanin [PDF]
European Journal of Biochemistry, 1995 The reaction that gives met‐hemocyanin from Octopus vulgaris oxy‐hemocyanin has been reinvesti‐gated under several experimental conditions. Various anions including azide, fluoride and acetate have been found to promote this reaction. Kinetic data indicate that the reaction mechanism is different from that currently accepted involving a peroxide ...
BELTRAMINI, MARIANO +5 more
openaire +3 more sources
Frontiers in Marine Science, 2019 The functional diversity of crustacean hemocyanins is broad, encompassing O2 delivery, innate immune response, metabolite storage, and osmolyte balance, all in a heterogeneous protein structure.
Jason Wang +2 more
doaj +1 more source
Biophysical characterization of the structural stability of Helix lucorum hemocyanin
Biotechnology & Biotechnological Equipment, 2021 The structural stability of the hеmocyanin purified from the hеmolymph of gаrden snаils Helix lucorum (HlH) was investigated by means of far-UV circular dichroism (CD), differential scanning calorimetry (DSC) and transmission electron microscopy (TEM ...
Krassimira Idakieva +5 more
doaj +1 more source
Food Science and Human Wellness, 2019 Human norovirus is the leading cause of foodborne illness globally. Detection and quantification of norovirus commonly involves the use of reverse transcriptase quantitative polymerase chain reaction (RT-qPCR); however, the presence of inhibitory ...
Cassandra Suther, Matthew D. Moore
doaj +1 more source
Frontiers in Marine Science, 2020 This study evaluated two approaches to the aquaculture of Limulus polyphemus with the ultimate goal of harvesting Limulus amebocyte lysate (LAL) at an industrial scale.
Rachel Tinker-Kulberg +14 more
doaj +1 more source
Hemocyanin-derived phenoloxidase activity is dependent on dodecameric structure in shrimp Litopenaeus vannamei [PDF]
Archives of Biological Sciences, 2015 Hemocyanin (Hc) is a multifunctional protein in both mollusks and arthropods. Phenoloxidase (PO) activities are the most important physiological functions for Hcs after conversion.
Wang Ke-Zhou +4 more
doaj +1 more source
Molluscan mega-hemocyanin: an ancient oxygen carrier tuned by a ~550 kDa polypeptide
Frontiers in Zoology, 2010 Background The allosteric respiratory protein hemocyanin occurs in gastropods as tubular di-, tri- and multimers of a 35 × 18 nm, ring-like decamer with a collar complex at one opening. The decamer comprises five subunit dimers.
Harasewych Myroslaw G +7 more
doaj +1 more source
Hemocyanin-derived phenoloxidase reaction products display anti-infective properties [PDF]
, 2018 Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme.
James Talbot +2 more
core +1 more source