Abstract
Rat liver poly(A)-containing RNA was translated in an ascites cell-free system. Labeled protein precipitable by antibody directed against rat serum albumin was identified as pre-proalbumin based on its size and partial NH2-terminal sequence. However, when an ascites membrane fraction was added to the translation reaction, the albumin antibody-precipitable material was smaller than pre-proalbumin. Partial NH2-terminal sequence analysis of this protein revealed that it was proalbumin. Conversion of pre-proalbumin to proalbumin by the ascites membrane fraction was complete and precise--i.e. no serum albumin was observed. Reconstitution in vitro of the processing of pre-proalbumin to its stable intracellular form, proalbumin, provides a method for studying the initial proteloytic event involved in secretion of rat serum albumin.
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