N-Terminal Amino Acid Sequence Comparison of Asian Horseshoe Crab Hemocyanins: Immunologically Identical Hemocyanin Subunits Are Orthologous in Asian Horseshoe Crabs
نویسندگان
چکیده
منابع مشابه
Hemocyanin of the Horseshoe Crab, Limzdus polyphemus
The high molecular weight hemocyanin found in the hemolymph of the horseshoe crab, Limulus polyphemus, is composed of at least eight different kinds of subunits. Ion exchange chromatography at high pH in the presence of EDTA yields five major zones, hemocyanins I to V, three of which are electrophoretically heterogeneous. The subunits have similar molecular weights, 65,000 to 70,000, and their ...
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Hemocyanin in the hemolymph of the horseshoe crab, Limulus polyphemus L., is a high-molecular-weight copper protein which binds oxygen cooperatively and shows a higher oxygen affinity at pH 7 than at pH 9. Treatment with EDTA (ethylenediaminetetra-acetate) disaggregates the hemocyanin molecules and abolishes both the reverse Bohr effect and cooperative oxygen binding. Chloride ions interact wit...
متن کاملIsolation and Characterization of a Sialic Acid - specific Southeast Asian Horseshoe Crab TkieJlypleus gigas Lectin from Hemolymph of the
masses of 31 kDa. The serological specificity of the purified lectin was specifically inhibited by siatic acids sialoglycoproteins, but not by neutral sugars, hexosamines, IV-acetylhexosamines, or asialoglycopreteins. A]though the N-terminal amino acid sequence of the 1ectin from T. gigas was identical to that frem American horseshoe crab (liphemin) by the same pllrification method and cross re...
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ژورنال
عنوان ژورنال: Zoological Science
سال: 1998
ISSN: 0289-0003
DOI: 10.2108/zsj.15.295