Abstract:
:Human liver alkaline phosphatase [ortho-phosphoric monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] was purified, and some of its physical and chemical properties were examined and compared to those of human placental alkaline phosphatase. The results indicated a different peptide structure for each, based upon HB2-terminal residue sequence, two-dimensional tryptic peptide maps, and different amino acid compositions. These data are interpreted to indicate that the enzymes are synthesized by different structural genes. Other molecular properties differentiating the two enzymes were a higher apparent molecular weight for the liver enzyme from sodium dodecyl sulfate gel electrophoresis, a higher S20,w value, different carbohydrate content, and a different isoelectric point. The immunochemical specificity of each enzyme was not affected by removal of sialic acid groups. Both enzymes are similar in that they are dimers of equal molecular weight subunits, and are probably homodimers.
journal_name
Proc Natl Acad Sci U S Aauthors
Badger KS,Sussman HHdoi
10.1073/pnas.73.7.2201keywords:
subject
Has Abstractpub_date
1976-07-01 00:00:00pages
2201-5issue
7eissn
0027-8424issn
1091-6490journal_volume
73pub_type
杂志文章abstract::A human lambdaV (Mcg) and a human lambdaII (Vil) myeloma protein have identical sequences in their first hypervariable segments although they differ at 21 positions throughout the variable region. If a different structural gene is responsible for each subgroup, the findings favor insertion of information for the hyper...
journal_title:Proceedings of the National Academy of Sciences of the United States of America
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doi:10.1073/pnas.72.12.5107
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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