Biomedical subjects

Isao Miyagawa

Publications and source records attributed to Isao Miyagawa.

3 recordsLinked to original sources

PubMed2006

Motion and shape recovery based on iterative stabilization for modest deviation from planar motion.

We describe an iterative stabilization method that can simultaneously recover camera motion and 3D shape from an image sequence captured under modest deviation from planar motion. This technique iteratively applies a factorization method based on planar motion and can approximate the observed image points to the 2D points projected under planar motion by stabilizing the camera motion. We apply the proposed method to aerial images acquired by a helicopter-borne camera and show better reconstruction of both motion and shape than Christy-Horaud's perspective factorization. Moreover, we confirm that the reprojection errors calculated from the recovered camera motion and 3D shape are very similar to the optimum results yielded by bundle adjustment.

Algorithms↗

PubMed2003

Arabidopsis 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase: cDNA cloning and expression analyses.

The molecular characterization of two isoforms of 3-deoxy-d-manno-oct-2-ulosonate (KDO) -8-phosphate synthase (AtkdsA1 and AtkdsA2) from Arabidopsis is reported here. First, by isolating a full-length cDNA for AtkdsA1, it was confirmed that the deduced primary structures of AtkdsA1 and AtkdsA2 proteins were 93% identical. Functional expression and purification studies demonstrated the efficient catalytic activity of the AtkdsA1 enzyme to produce KDO-8-phosphate from phosphoenolpyruvate and d-arabinose-5-phosphate. RT-PCR and RNA-gel blot analysis revealed different expression profiles for both genes; the AtkdsA1 gene was predominantly expressed in the shoots, while the AtkdsA2 transcript accumulated to a higher level in the roots, implicating differential roles of these isoforms in planta.

Aldehyde-Lyases↗

PubMed2002

Purification and cDNA cloning of UDP-D-glucuronate carboxy-lyase (UDP-D-xylose synthase) from pea seedlings.

Uridine diphospho-D-glucuronate carboxy-lyase (UDP-D-xylose synthase; EC 4.1.1.35), which catalyzes the conversion of UDP-D-glucuronate to UDP-D-xylose, was purified to apparent homogenity from pea (Pisum sativum L.) seedlings. The pH optimum for enzyme activity was around 5-6, and the activity was not affected by exogeneously supplied NAD+ and NADH. The purified enzyme had a molecular weight of 250 kDa and consisted of 42 kDa polypeptides. Based on the amino acid sequence, a probe (400 bp) was prepared with degenerate primers by a reverse transcriptase-PCR. Using this probe, a clone encoding 346 amino acid residues was screened from a pea cDNA library. The recombinant protein expressed in Escherichia coli catalyzed conversion of UDP-D-glucuronate to UDP-D-xylose, confirming that the isolated clone encoded UDP-D-glucuronate carboxy-lyase.

Amino Acid Sequence↗