{'fraction_non_alphanumeric': 0.02583732057416268, 'fraction_numerical': 0.0, 'mean_word_length': 5.378048780487805, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Comparative electrophoretic analysis of the virus proteins of four rhabdoviruses.

Summary
The structural proteins of vesicular stomatitis virus (VSV) Indiana, VSV New Jersey, Chandipura virus and Piry virus were compared by using two different SDS-polyacrylamide gel electrophoresis systems. The G and M proteins of the Indiana serotype had different electrophoretic mobilities from the corresponding proteins of VSV New Jersey, Chandipura virus and Piry virus in a continuous-SDS (CONT-SDS) gel system. The three major proteins of VSV Indiana G, N and M, were distinctly different from their counterpart proteins in the other three viruses when a high-resolution discontinuous-SDS (DISC-SDS) system was used. Chandipura and Piry virus glycoproteins migrated differently when co-electrophoresed in the CONT-SDS system, whereas both their N and M proteins were different in the DISC-SDS method. During infection both Chandipura and Piry viruses produced defective T particles which contained the same four structural proteins as virus particles.