56 results match your criteria: "Tsukuba Center[Affiliation]"

Structures of biological surfaces pressed on to a pure liquid gallium surface were successfully traced on to the gallium surface by quick-freezing below the melting point (28.78 degrees C) in air or water for replication in scanning electron microscopy. Gallium's high surface tension (approximately 700 mN m(-1) at 30 degrees C) deteriorates the spatial resolution of replicas and destroys some types of specimens.

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A technique using pure gallium metal as a replication material is reported for biological surface scanning electron microscopy (SEM). The technique first directly enables aquatic organisms in water to be replicated due to gallium's low melting point and, second, reproduces surface structures and images of the two-dimensional (2D) distribution of substances transferred from the original surface to the gallium surface due to gallium's high surface tension. An aquatic protozoan in water was directly replicated to show its typical surface structures.

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Giant hemoglobin (Hb) from Perinereis aibuhitensis is made of several types of protein components including single-chain globin (a), disulfide-bridged globin trimer (A-b-B), disulfide-bridged dimers of nonglobin chain (or linkers; L1-L1, L2-L2, and L1-L2), and oligomers of L1-L2 [(L1-L2)n]. The intact form of this giant Hb is a two-tiered hexagonal structure composed of 12 identical units, or so-called submultiples (six submultiples to a tier). To obtain a view of the three-dimensional architectural arrangement of these components in the intact form, we identified the subunit loci by using two mutually complementary chemical modifications and a colloidal gold labeling technique.

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Wheat germ agglutinin-reactive chains of multisubunit extracellular hemoglobin from the polychaete Perinereis aibuhitensis were identified to clarify the carbohydrate gluing which is the carbohydrate-dependent supramolecular architecture of the hemoglobin (Ebina S. et al. (1995) Proc.

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Two alternative forms of cDNA encoding CD34.

Exp Hematol

February 1993

Laboratory of Cell Growth and Differentiation, Life Science Tsukuba Center, Ibaraki, Japan.

By expression cloning using FACS, we have isolated cDNA clones encoding human CD34 from a megakaryoblastoid cell line. The predicted amino acid sequence of CD34 revealed the type I transmembrane protein consisted of a leader peptide (31 residues), an extracellular domain (258 residues), a transmembrane domain (23 residues) and a cytoplasmic domain of 73 residues. In addition, a second form of cDNA that has 194 bp insertion in the cytoplasmic region was isolated.

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