{'fraction_non_alphanumeric': 0.02034587995930824, 'fraction_numerical': 0.013224821973550356, 'mean_word_length': 5.431372549019608, '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}}
Elastogenesis and microfibrillar glycoprotein synthesis by bovine ligamentum nuchae cells in culture.

Cell cultures propagated from fetal bovine ligamentum nuchae were found to accumulate an extensive extracellular matrix containing collagen and elastic fibers when maintained for periods up to 8 weeks. The synthesis by these cells of two glycoproteins, designated MFP I and MFP II, which are immunologically related to components of the elastic fiber microfibrils was investigated. MFP II, apparent mol. t. 300,000, was shown to be a non-collagenous glycoprotein whereas MFP I, apparent mol. wt. 150,000, was found to be a novel collagenous glycoprotein containing hydroxyproline and glycosylated hydroxylysine residues but exhibiting properties of distinct from the known collagens. Two glycoproteins having characteristics similar to MFP I and MFP II were also identified in an extract of the cell layer and in a "microfibrillar protein preparation" from intact nuchal ligament.