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Quantification of p38/synaptophysin in highly purified adrenal medullary chromaffin vesicles
Author(s) -
Schilling K.,
Gratzl M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81348-6
Subject(s) - synaptophysin , vesicle , percoll , differential centrifugation , chromaffin cell , synaptic vesicle , organelle , chemistry , biology , biophysics , centrifugation , biochemistry , adrenal medulla , endocrinology , catecholamine , immunology , membrane , immunohistochemistry
Chromaffin vesicles were first purified by differential and density gradient centrifugation in isotonic (Percoll) gradients. In subsequent sucrose gradients p38/synaptophysin exhibited the same distribution as established marker substances of chromaffin vesicles. Quantification of immunoblots revealed that 750 ng p38/synaptophysin per mg of protein were present in the chromaffin vesicles recovered from the sucrose gradient. Thus the amount of p38/synaptophysin per mg protein of chromaffin vesicles is about 100 times lower than that observed in clear (synaptic) vesicles. However, because of the large difference in surface area and protein content, the amount of p38/synaptophysin per single vesicle is the same in both types of organelles.