Title : Processing of rat and human
angiotensinogen precursors by microsomal membranes
Abstract :
- We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation
- Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B
- 35S- Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S- methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography
- N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin
- For rat angiotensinogen , only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized
- For neither rat or human angiotensinogen precursor was there any evidence for a prosequence
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. N-glycosylation, , -, -, sites
- 1. asparagine-linked, , -, asparagine-linked oligosaccharide units, asparagine
- 3. glycosylated, , angiotensinogen, -, -
- 3. nonglycosylated, , angiotensinogen, -, -
- 4. N-Glycosylation, , angiotensinogen, -, -
- 5. N-glycosylation, , -, -, sites
- 5. N-glycosylation, , angiotensinogen, -, -
- 5. utilized, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):