Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma

Tomita, Y. ; Hariu, A. ; Kato, C. ; Seiji, M.

Amsterdam : Elsevier
ISSN:
0003-9861
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798292172217253888
autor Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
autorsonst Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
book_url http://dx.doi.org/10.1016/0003-9861(83)90008-5
datenlieferant nat_lic_papers
fussnote The transfer of tyrosinase from microsomes into melanosomes, without passing through the cytosol in the Harding-Passey mouse melanoma cell, was confirmed by experiments carried out using a combination of radioisotope tracer techniques and immunoprecipitation. ^3H-Labeled amino acid incorporation into tyrosinase present in the microsome, melanosome, and soluble fractions confirmed the precursor-product relationship of the enzyme in the microsome fraction and in the melanosome fraction. However, two forms of the enzyme, T"s"1- and T"s"2-tyrosinase, separated from the soluble fraction by polyacrylamide gel electrophoresis, were shown to play no role in the transfer since little or no incorporation of radioactivity into tyrosinase in this fraction was found. It is suggested that most tyrosinase observed in the soluble fraction does not leak from the melanosomes or the microsomes during homogenization, but comes from necrotic tumor cells. It appears that melanosomal and microsomal tyrosinase might be released from the membrane of necrotic cells modified by various degradation enzymes, considering the data on the recovery of tyrosinase from the soluble fraction, where one-third of total enzyme activity in the postnuclear fraction could not be increased, even when the postnuclear fraction of the tumor was further homogenized radically.
hauptsatz hsatz_simple
identnr NLZ183811119
issn 0003-9861
journal_name Archives of Biochemistry and Biophysics
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 225 (1983), S. 75-85
search_space articles
shingle_author_1 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
shingle_author_2 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
shingle_author_3 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
shingle_author_4 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
shingle_catch_all_1 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
0003-9861
00039861
Elsevier
shingle_catch_all_2 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
0003-9861
00039861
Elsevier
shingle_catch_all_3 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
0003-9861
00039861
Elsevier
shingle_catch_all_4 Tomita, Y.
Hariu, A.
Kato, C.
Seiji, M.
Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
0003-9861
00039861
Elsevier
shingle_title_1 Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
shingle_title_2 Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
shingle_title_3 Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
shingle_title_4 Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
sigel_instance_filter dkfz
geomar
wilbert
ipn
albert
fhp
source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:44:17.150Z
titel Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
titel_suche Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
The transfer of tyrosinase from microsomes into melanosomes, without passing through the cytosol in the Harding-Passey mouse melanoma cell, was confirmed by experiments carried out using a combination of radioisotope tracer techniques and immunoprecipitation. ^3H-Labeled amino acid incorporation into tyrosinase present in the microsome, melanosome, and soluble fractions confirmed the precursor-product relationship of the enzyme in the microsome fraction and in the melanosome fraction. However, two forms of the enzyme, T"s"1- and T"s"2-tyrosinase, separated from the soluble fraction by polyacrylamide gel electrophoresis, were shown to play no role in the transfer since little or no incorporation of radioactivity into tyrosinase in this fraction was found. It is suggested that most tyrosinase observed in the soluble fraction does not leak from the melanosomes or the microsomes during homogenization, but comes from necrotic tumor cells. It appears that melanosomal and microsomal tyrosinase might be released from the membrane of necrotic cells modified by various degradation enzymes, considering the data on the recovery of tyrosinase from the soluble fraction, where one-third of total enzyme activity in the postnuclear fraction could not be increased, even when the postnuclear fraction of the tumor was further homogenized radically.
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