| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-51 |
Sentence |
denotes |
Arrangement of human erythrocyte membrane proteins. |
| T2 |
52-254 |
Sentence |
denotes |
The orientation of human erythrocyte membrane protein was examined by enzymic iodination using lactoperoxidase with the glucose-oxidase system for generating peroxide, followed by proteolytic digestion. |
| T3 |
255-440 |
Sentence |
denotes |
The outer surface of intact cells was labeled with 125I and the cytoplasmic surface of either resealed ghosts containing lactoperoxidase or of inside-out vesicles was labeled with 131I. |
| T4 |
441-617 |
Sentence |
denotes |
Following iodination, the outer surface (resealed ghosts) or the cytoplasmic surface (outer surface of inside-out vesicles) was digested with trypsin, chymotrypsin, or pronase. |
| T5 |
618-749 |
Sentence |
denotes |
Sodium dodecyl sulfate gel electrophoresis of the isolated membranes revealed three major and several minor peaks of radioactivity. |
| T6 |
750-1373 |
Sentence |
denotes |
Their surface orientation, defined within the limits of the specificity of the probes used, was as follows: the three major peaks consist of: (a) a 90,000 to 100,000 molecular weight component labeled on both surfaces; its proteolytic digestion profile indicated that it spans the membrane in an asymmetric manner and that it is composed of more than one peptide; (b) the major red cell membrane glycoprotein (apparent molecular weight 60,000) which is labeled and digested at only the outer surface; and (c) peptide(s) of high molecular weight (approximately 200,000), labeled and digested at only the cytoplasmic surface. |
| T7 |
1374-1602 |
Sentence |
denotes |
The minor components include a glycoprotein of approximately 25,000 (apparent molecular weight) accessible to both surfaces and peptides of 60,000 to 70,000, 45,000, and 20,000 molecular weight labeled only on the inner surface. |
| T1 |
0-51 |
Sentence |
denotes |
Arrangement of human erythrocyte membrane proteins. |
| T2 |
52-254 |
Sentence |
denotes |
The orientation of human erythrocyte membrane protein was examined by enzymic iodination using lactoperoxidase with the glucose-oxidase system for generating peroxide, followed by proteolytic digestion. |
| T3 |
255-440 |
Sentence |
denotes |
The outer surface of intact cells was labeled with 125I and the cytoplasmic surface of either resealed ghosts containing lactoperoxidase or of inside-out vesicles was labeled with 131I. |
| T4 |
441-617 |
Sentence |
denotes |
Following iodination, the outer surface (resealed ghosts) or the cytoplasmic surface (outer surface of inside-out vesicles) was digested with trypsin, chymotrypsin, or pronase. |
| T5 |
618-749 |
Sentence |
denotes |
Sodium dodecyl sulfate gel electrophoresis of the isolated membranes revealed three major and several minor peaks of radioactivity. |
| T6 |
750-1373 |
Sentence |
denotes |
Their surface orientation, defined within the limits of the specificity of the probes used, was as follows: the three major peaks consist of: (a) a 90,000 to 100,000 molecular weight component labeled on both surfaces; its proteolytic digestion profile indicated that it spans the membrane in an asymmetric manner and that it is composed of more than one peptide; (b) the major red cell membrane glycoprotein (apparent molecular weight 60,000) which is labeled and digested at only the outer surface; and (c) peptide(s) of high molecular weight (approximately 200,000), labeled and digested at only the cytoplasmic surface. |
| T7 |
1374-1602 |
Sentence |
denotes |
The minor components include a glycoprotein of approximately 25,000 (apparent molecular weight) accessible to both surfaces and peptides of 60,000 to 70,000, 45,000, and 20,000 molecular weight labeled only on the inner surface. |
