| 영문 | hemoglobin | 한글 | 혈색소 |
|---|---|---|---|
| 설명 | 척추동물의 적혈구 속에 다량으로 들어있는 색소단백질. 철을 품는 포르피린 고리와 단백질의 일종(글로빈)으로 되어 있다. 철(Fe)에는 산소와 가역적으로 결합하는 능력이 있어, 생체 내에서는 산소를 운반하는 일을 한다. 혈색소 한 분자는 네 개의 폴리펩티드 사슬로 되어 있고, 각각의 폴리펩티드 사슬에는 한 개씩의 헴이 함유되어 있다. 따라서 혈색소 한 분자에는 철원자가 네 개 함유되고, 철원자 한 개에 대해 한 분자씩의 산소가 결합하므로, 혈색소 한 분자에는 산소 4분자가 결합한다. 혈색소는 산소압이 높은 허파나 아가미에서는 산소와 결합하고, 산소압이 낮은 조직에 이르면 산소를 유리한다. 더욱이 산소의 방출은 pH가 낮아짐에 따라 촉진되므로, 이산화탄소가 많고 pH가 낮은 말초조직에서는 산소를 보다 유리하기 쉽게 된다. 이산화탄소는 혈장 속에 녹아 허파에 운반되어 허파호흡으로 체외에 방출되면 pH는 다시 원상태로 돌아가고 혈색소는 다시 산소와 결합한다. 분자량 약 6,500의 색소단백질로 혈액 속에서의 함유량은 혈액 100 mL중의 그램수로 나타낸다. 정상치는 남자 16g/dL(14~18g/dL), 여자 14g/dL (12~16g/dL)이다. |
||
| HbA | hemoglobin A, adult hemoglobin |
|---|---|
| HbF | fetal hemoglobin, hemoglobin F |
| HBGR | hemoglobin-gamma regulator HbH hemoglobin H |
| HbS | hemoglobin S, sickle-cell hemoglobin |
| HbZ | hemoglobin Z, hemoglobin Zurich |
| CASE | Computer Automated Structure Evaluation |
|---|---|
| DLS | Dimer Linkage Structure |
| EXAFS | Extended X-Ray Absorption Fine Structure |
| QSAR | Quantitative Structure Activity Relationship |
| QSPR | Quantitative Structure-Property Relationship |
| hemoglobin | <cell biology, haematology> Four subunit globular oxygen carrying protein of the erythrocytes of vertebrates and some invertebrates. It is a conjugated protein containing four haem groups and globin. There are two alpha and two beta chains (very similar to myoglobin) in adult humans, the haem moiety (an iron containing substituted porphyrin) is firmly held in a nonpolar crevice in each peptide chain. There are four globin polypeptide chains, designated alpha, beta, gamma, delta in the adult. Each is composed of several hundred amino acids. (08 Mar 2000) |
|---|---|
| brush heap structure | Haphazard interlocking of fibrils in a gel or hydrocolloid impression material. (05 Mar 2000) |
| gel structure | Brush heap structure of fibrils giving firmness to hydrocolloids. (05 Mar 2000) |
| genetic fine structure | The study of genes on the level of their nucleotide sequences and what happens to their molecular structure at that level. (09 Oct 1997) |
| chi structure | <molecular biology> The name for the X-shaped structure which forms during the recombination process between two plasmids, or circular pieces, of DNA. The Greek letter chi resembles this structure. (05 Jan 1998) |
| group structure | The informal or formal organization of a group of people based on a network of personal relationships which is influenced by the size and composition, etc., of the group. (12 Dec 1998) |
| molecular structure | The location of the atoms, groups or ions relative to one another in a molecule, as well as the number and location of chemical bonds. (12 Dec 1998) |
| cointegrate structure | A structure of DNA produced by the fusion of two replicons, one possessing a transposon. (05 Mar 2000) |
| cruciform structure | A structure, shaped like a cross, which can form during homologous recombination when inverted base-pair repeats pair with each other on the same strand of DNA instead of with homologous sections on a different strand of DNA. (09 Oct 1997) |
| crystal structure | <chemistry> The configuration in which atoms are arranged in a material. These arrangements have a direct effect on the physical properties of the material. These arrangements commonly take the form of cubes, rectangular solids, hexagonal solids. Etc. (05 Aug 1998) |
| primary structure | The covalent backbone of a macromolecule. The order of subunits in a biological polymer, such as amino acids in a polypeptide or nucleotides in a molecule of DNA or RNA. (09 Oct 1997) |
| protein structure | The amino acids and their manner of arrangement in constituting a protein. The four stages of protein structuring are primary (protein structure, primary see amino acid sequence), secondary (protein structure, secondary), tertiary (protein structure, tertiary), and quaternary (protein structure, quaternary see protein conformation). (12 Dec 1998) |
| protein structure, secondary | The stage in the development of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices and beta sheets. This is the first folding level of protein building. (12 Dec 1998) |
| protein structure, tertiary | The stage in the structural development of a protein in which combinations of alpha helices and beta sheets pack together to form compactly folded globular units named domains. Small proteins consist of only one domain but larger proteins contain a number of domains which are usually connected by open lengths of polypeptide chain. This stage is a combination of the second and third folding levels of protein building. (12 Dec 1998) |
| secondary structure | <molecular biology> Structures produced in polypeptide chains involving interactions between amino acids within the chain. Especially _ helical and _ pleated sheet structures. Also applies to the complex folding of nucleic acids as, for example: the clover leaf structure of tRNA. (18 Nov 1997) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|