Transfer of tyrosinase to melanosomes in Harding-Passey mouse melanoma
ISSN: |
0003-9861
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
Physics
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798292172217253888 |
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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. |
topic | W V U |
uid | nat_lic_papers_NLZ183811119 |