Search PubMed⌕ Search

Biomedical subjects

K Fukasawa

Publications and source records attributed to K Fukasawa.

105 records · Page 6Linked to original sources
PubMed1981

Phosphoprotein phosphatase activity of bovine intestinal alkaline phosphatase.

The phosphoprotein phosphatase activity of a commercial preparation of bovine intestinal alkaline phosphatase (EC 3.1.3.1) was examined using phosvitin and dentine phosphoprotein as substrates. Over 90% and 70% of the phosphorus from dentine phosphoprotein and phosvitin were hydrolyzed in 2 h. The optimum pH of the enzyme for the dephosphorylation of phosvitin and dentine phosphoprotein was nearly 6. No protein phosphatase activity was observed when the alkaline phosphatases from bovine liver and pulp were investigated.

Alkaline Phosphatase↗
PubMed1981

Immunohistochemical localization of dipeptidyl aminopeptidase IV in rat kidney, liver, and salivary glands.

Specific antibodies directed against dipeptidyl aminopeptidase (DAP) IV prepared from rat and pig kidneys were produced in rabbits. Using a peroxidase-labeled or fluorescein isothiocyanate-labeled antibody method, localization of DAP IV was investigated in various tissues of the rat (kidney, liver and salivary glands). DAP IV was mainly localized in the brush border of the proximal tubules (kidney), in the cell membrane around bile canaliculi of hepatic cells (liver), and in the cell membrane of serous acinar cells (parotid and submaxillary glands). These results substantiate that DAP IV is a membrane-bound peptidase.

Animals↗
PubMed1980

Identification and quantification of alpha-amino adipic acid in bovine dentine phosphoprotein.

A unique phosphoprotein, which contains an uncommon amino acid, alpha-amino adipic acid (alpha-AAA), was isolated from unerupted bovine teeth by extensive EDTA demineralization. The alpha-AAA in the protein hydrolysates was identified based on the elution time on an amino acid analyzer using the sodium and lithium citrate buffer in a dual column system, and its identity was confirmed by comparisons of its DNS derivative with that of authentic alpha-AAA. This result suggests that the lysine residues in the phosphoprotein may be deaminated by an amine oxidase into allysine and further oxidized to alpha-AAA.

2-Aminoadipic Acid↗
PubMed1978

Successive cleavage of N-terminal Arg1--Pro2 and Lys3-Pro4 from substance P but no release of Arg1-Pro2 from bradykinin, by X-Pro dipeptidyl-aminopeptidase.

X-Pro dipeptidyl-aminopeptidase (EC 3.4.14.1) purified homogeneously from the human submaxillary gland was proved to hydrolyze N-terminal dipeptide Arg1-Pro2 and subsequent dipeptide Lys3-Pro4 from substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-gly-Leu-Met-NH2). Km and V values of hydrolysis of substance P were 2.0 mM and 3.6 mumol/min per mg protein, respectively. In contrast, the N-terminal Arg-Pro of bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) was not cleaved by the enzyme.

Amino Acid Sequence↗
PubMed1978

Dipeptidyl aminopeptidase IV, a glycoprotein from pig kidney.

Dipeptidyl aminopeptidase IV was purified 350 fold from pig kidney by chromatographic procedures including affinity chromatography with conjugates of Gly-Pro linked to Sepharose 4.B. Purified enzyme existed in a dimeric form as determined by sodium dodecyl sulfate polyacrylamide-gel electrophoresis using dimethyl suberimidate (a cross-linking reagent). The molecular weight of the subunit was estimated to be 100 000 by gel filtration with 6 M guanidine hydrochloride and to be 94 000 based on analysis of N-terminal residue (dinitrophenyl-serine). The amino acid composition of the purified enzyme was also determined. The enzyme contained 18.3% of carbohydrate consisting of mannose, galactose, fucose, glucosamine and sialic acid. The enzyme desialized with sialidase was found to still possess full enzyme activity.

Amino Acids↗