TY - JOUR
T1 - Partial amino acid sequence of human placental lactogen precursor and its mature hormone form produced by membrane-associated enzyme activity
AU - Birken, Steven
AU - Smith, Donna L.
AU - Canfield, Robert E.
AU - Boime, Irving
N1 - Funding Information:
by NIH grant
PY - 1977/1/10
Y1 - 1977/1/10
N2 - The precursor form of human placental lactogen, synthesized by a wheat germ extract cell-free system, has been partially sequenced and found to contain a high percentage of leucine residues within its first 20 amino acids. The partial NH2-terminal structure appears to be: {A figure is presented} The precursor form of hPL, produced by an ascites extract cell-free system, was cleaved by a membrane-associated enzyme into a form which exhibits the methionine and valine residues in NH2-terminal positions identical to those of native human placental lactogen.
AB - The precursor form of human placental lactogen, synthesized by a wheat germ extract cell-free system, has been partially sequenced and found to contain a high percentage of leucine residues within its first 20 amino acids. The partial NH2-terminal structure appears to be: {A figure is presented} The precursor form of hPL, produced by an ascites extract cell-free system, was cleaved by a membrane-associated enzyme into a form which exhibits the methionine and valine residues in NH2-terminal positions identical to those of native human placental lactogen.
UR - http://www.scopus.com/inward/record.url?scp=0017576876&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(77)91381-X
DO - 10.1016/0006-291X(77)91381-X
M3 - Article
C2 - 836272
AN - SCOPUS:0017576876
VL - 74
SP - 106
EP - 112
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -