A novel protein with alkaline phosphatase and protease inhibitor activities in Streptomyces hiroshimensis.
A novel alkaline phosphatase (S-ALP) was found in the culture filtrate of Streptomyces hiroshimensis IFO 12785. Purification was achieved on Sephadex G-75 column, palmitoylated gauze column, and Superdex 75 HR column chromatographies. The molecular weight of S-ALP was estimated to be 14200 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The isoelectric point is 9.2. S-ALP had maximum enzyme activity at pH 9.5. S-ALP efficiently catalyzed both p-nitrophenyl phosphate and p-nitrophenyl phosphorylcholine substrates, particularly the latter. The N-terminal amino acid sequence (25 residues) of S-ALP was 60 to 72% identical to that of Streptomyces subtilisin inhibitor-like proteins. S-ALP exhibited trypsin inhibition in addition to a strong inhibition of subtilisin.
Second Department of Hygienic Chemistry, Tohoku Pharmaceutical University, Sendai, Miyagi, Japan.
Masayuki
M
Nitta
Mariko
M
Goto
Naomi
N
Shibuya
Yoshio
Y
Okawa
D000469:Alkaline Phosphatase / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002384:Catalysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013302:Streptomyces / Q000737:chemistry* / Q000254:growth & development; D013379:Substrate Specificity; D020860:Subtilisin / Q000037:antagonists & inhibitors; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology
D001426:Bacterial Proteins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D000469:Alkaline Phosphatase; D020860:Subtilisin