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Why Is Protein Cleaved By Signal Peptidase?

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Why Is Protein Cleaved By Signal Peptidase?
In order for the prolactin single peptide to enter the ER lumen and be cleaved by signal peptidase, the prolactin nascent chain must be 130 codons. The mRNA at size 130 codons in length is seen to have cleavage in the presence of microsomes. The shorter sized mRNA’s in the presence of microsomes, are the non cleaved residue peptides in which the signal peptidase is unable to cleave the signal sequence amino acid.
B. Band B is the cleavage of the signal sequence by the signal peptidase. The cleavage of the polypeptide weighs less then when the protein was attached to the signal sequence and before it grows in the ER lumen. This is evident from the diagram, since lighter proteins move father down the gel than do heavier ones.

Given the length

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