TY - JOUR
T1 - Liver-like alkaline phosphatase in the tissue-unspecific type enzyme found in rabbit organs
AU - Koyama, Iwao
AU - Fujimori-Arai, Yoko
AU - Hirota, Norio
AU - Sakai, Takao
AU - Sakagishi, Yoshikatsu
AU - Komoda, Tsugikazu
N1 - Funding Information:
This work was supportedin a Dart bv ~rant0 267107? (T.K.) from the Ministry of Education, Science and Culture of Japan and a grant from Nisshin Flour Milling Co, (Tokyo1.
PY - 1991/10/25
Y1 - 1991/10/25
N2 - Rabbit liver and kidney tissues are known to produce an intestinal-like alkaline phosphatase (IAP-like enzyme) as a dominant isozyme, with a minor isozyme of tissue-unspecific type (UAP), unlike humans and other mammalians. We investigated immunohistochemically and biochemically these unique isozymes in the rabbit liver and bone, and compared them with the human isozyme. In rabbit liver, UAP was found to be localized only in the apical part of the membrane of cells lining the bile duct, whereas IAP-like enzyme was found in the sinusoidal membrane of hepatocytes. Rabbit liver UAP was separated from IAP-like enzyme by DEAE-cellulose column chromatography. Rabbit bone tissue contained only one UAP isozyme. The two UAPs were biochemically and physicochemically compared with human liver AP. Both UAPs reacted with an anti-human liver AP monoclonal antibody, not with an anti-human bone AP monoclonal antibody, indicating that both enzymes have the same antigenicity as human liver AP. Rabbit liver and bone UAPs had similar N-linked sugar-chain heterogeneities to the respective human enzymes. In addition, rabbit bone AP also had an O-linked sugar chain, as did human bone AP, unlike rabbit and human liver APs.
AB - Rabbit liver and kidney tissues are known to produce an intestinal-like alkaline phosphatase (IAP-like enzyme) as a dominant isozyme, with a minor isozyme of tissue-unspecific type (UAP), unlike humans and other mammalians. We investigated immunohistochemically and biochemically these unique isozymes in the rabbit liver and bone, and compared them with the human isozyme. In rabbit liver, UAP was found to be localized only in the apical part of the membrane of cells lining the bile duct, whereas IAP-like enzyme was found in the sinusoidal membrane of hepatocytes. Rabbit liver UAP was separated from IAP-like enzyme by DEAE-cellulose column chromatography. Rabbit bone tissue contained only one UAP isozyme. The two UAPs were biochemically and physicochemically compared with human liver AP. Both UAPs reacted with an anti-human liver AP monoclonal antibody, not with an anti-human bone AP monoclonal antibody, indicating that both enzymes have the same antigenicity as human liver AP. Rabbit liver and bone UAPs had similar N-linked sugar-chain heterogeneities to the respective human enzymes. In addition, rabbit bone AP also had an O-linked sugar chain, as did human bone AP, unlike rabbit and human liver APs.
UR - https://www.scopus.com/pages/publications/0025944950
UR - https://www.scopus.com/pages/publications/0025944950#tab=citedBy
U2 - 10.1016/0167-4838(91)90145-P
DO - 10.1016/0167-4838(91)90145-P
M3 - Article
C2 - 1932093
AN - SCOPUS:0025944950
SN - 0167-4838
VL - 1080
SP - 165
EP - 172
JO - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
JF - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
IS - 2
ER -