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H R Colten

Publications and source records attributed to H R Colten.

208 records · Page 12Linked to original sources
PubMed1968

Synthesis of the first component of human complement in vitro.

Isolated segments of human colon and to a lesser extent ileum were capable of synthesizing hemolytically active C'1. This conclusion was based on the following evidence: After elimination of C'1 from tissue with EDTA, we found that segments of the intestinal tract in short-term organ culture showed a 50-1000-fold increase in C'1 activity. The rate of production of C'1 in human intestine was highly temperature dependent; C'1 production was reversibly inhibited by puromycin and actinomycin D. Furthermore, (14)C-labeled amino acids were incorporated into molecules which behaved like C'1. No significant C'1(hu) synthesis was observed in isolated segments of jejunum, stomach, liver, kidney, lung, spleen, lymph node, and thymus.

Amino Acids↗
PubMed1967

Efficiency of the first component of complement (C'1) in the hemolytic reaction.

With the use of the first component of guinea pig complement (C'1) labeled in vivo with (14)C-amino acids, we have obtained evidence that, under the conditions required for the assay of C'1, each molecule of C'1 capable of interaction with cell surface antigen-antibody complexes is capable of initiating the reaction sequence that leads to lysis of the cell.

Animals↗
PubMedDate not supplied

Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.

Gelsolin is representative of a class of actin-modulating proteins found in lower eukaryotes to mammals, which sever actin filaments. Gelsolin found in the cytoplasm of cells is functionally similar to a mammalian plasma protein of similar size, originally called ADF or brevin. Human plasma and rabbit macrophage gelsolins differ by the presence of a 25-amino-acid residue extension on plasma gelsolin which appears to account for the difference in relative molecular mass (Mr) between the proteins as assessed by SDS-polyacrylamide gel electrophoresis (PAGE), 93,000 (93K) and 90K, respectively. Here we report the isolation of full-length human plasma gelsolin complementary DNA clones from a HepG2 library. The inferred amino-acid sequence reveals the presence of a signal peptide, a long tandem repeat that matches the actin-binding domains of gelsolin, a tetrapeptide present in actin and extended regions of identical sequence with rabbit macrophage gelsolin. Southern blot analysis indicates that a single gene in the haploid genome encodes both protein forms.

Amino Acid Sequence↗