| ¿µ¹® | hemoglobin | ÇÑ±Û | Ç÷»ö¼Ò |
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| ¼³¸í | ôÃßµ¿¹°ÀÇ ÀûÇ÷±¸ ¼Ó¿¡ ´Ù·®À¸·Î µé¾îÀÖ´Â »ö¼Ò´Ü¹éÁú. öÀ» ǰ´Â Æ÷¸£ÇǸ° °í¸®¿Í ´Ü¹éÁúÀÇ ÀÏÁ¾(±Û·Îºó)À¸·Î µÇ¾î ÀÖ´Ù. ö(Fe)¿¡´Â »ê¼Ò¿Í °¡¿ªÀûÀ¸·Î °áÇÕÇÏ´Â ´É·ÂÀÌ ÀÖ¾î, »ýü ³»¿¡¼´Â »ê¼Ò¸¦ ¿î¹ÝÇÏ´Â ÀÏÀ» ÇÑ´Ù. Ç÷»ö¼Ò ÇÑ ºÐÀÚ´Â ³× °³ÀÇ Æú¸®ÆéƼµå »ç½½·Î µÇ¾î ÀÖ°í, °¢°¢ÀÇ Æú¸®ÆéƼµå »ç½½¿¡´Â ÇÑ °³¾¿ÀÇ ÇðÀÌ ÇÔÀ¯µÇ¾î ÀÖ´Ù. µû¶ó¼ Ç÷»ö¼Ò ÇÑ ºÐÀÚ¿¡´Â ö¿øÀÚ°¡ ³× °³ ÇÔÀ¯µÇ°í, ö¿øÀÚ ÇÑ °³¿¡ ´ëÇØ ÇÑ ºÐÀÚ¾¿ÀÇ »ê¼Ò°¡ °áÇÕÇϹǷÎ, Ç÷»ö¼Ò ÇÑ ºÐÀÚ¿¡´Â »ê¼Ò 4ºÐÀÚ°¡ °áÇÕÇÑ´Ù. Ç÷»ö¼Ò´Â »ê¼Ò¾ÐÀÌ ³ôÀº ÇãÆÄ³ª ¾Æ°¡¹Ì¿¡¼´Â »ê¼Ò¿Í °áÇÕÇϰí, »ê¼Ò¾ÐÀÌ ³·Àº Á¶Á÷¿¡ À̸£¸é »ê¼Ò¸¦ À¯¸®ÇÑ´Ù. ´õ¿íÀÌ »ê¼ÒÀÇ ¹æÃâÀº pH°¡ ³·¾ÆÁü¿¡ µû¶ó ÃËÁøµÇ¹Ç·Î, ÀÌ»êÈź¼Ò°¡ ¸¹°í pH°¡ ³·Àº ¸»ÃÊÁ¶Á÷¿¡¼´Â »ê¼Ò¸¦ º¸´Ù À¯¸®Çϱ⠽±°Ô µÈ´Ù. ÀÌ»êÈź¼Ò´Â Ç÷Àå ¼Ó¿¡ ³ì¾Æ ÇãÆÄ¿¡ ¿î¹ÝµÇ¾î ÇãÆÄÈ£ÈíÀ¸·Î ü¿Ü¿¡ ¹æÃâµÇ¸é pH´Â ´Ù½Ã ¿ø»óÅ·Πµ¹¾Æ°¡°í Ç÷»ö¼Ò´Â ´Ù½Ã »ê¼Ò¿Í °áÇÕÇÑ´Ù. ºÐÀÚ·® ¾à 6,500ÀÇ »ö¼Ò´Ü¹éÁú·Î Ç÷¾× ¼Ó¿¡¼ÀÇ ÇÔÀ¯·®Àº Ç÷¾× 100 mLÁßÀÇ ±×·¥¼ö·Î ³ªÅ¸³½´Ù. Á¤»óÄ¡´Â ³²ÀÚ 16g/dL(14~18g/dL), ¿©ÀÚ 14g/dL (12~16g/dL)ÀÌ´Ù. |
||
| 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 |
| DCLHb | Diaspirin Cross-Linked Hemoglobin |
|---|---|
| GHb | Glycosylated Hemoglobin |
| HbA1C | Hemoglobin A1C |
| Hb A2 | Hemoglobin A2 |
| HBOC | Hemoglobin-based oxygen carrier |
| 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) |
|---|---|
| haemoglobin Anti-Lepore | A group of abnormal haemoglobins similar to haemoglobin Lepore. These haemoglobins have normal a chains, but the non-a chain consists of the N-terminal portion of the b chain joined to the C-terminal portion of the d chain. This is the opposite crossing over pattern observed in haemoglobin Lepore. Examples of haemoglobin Anti-Lepore include HbMiyada, Hb PCongo, Hb PNilotic, and HbLincoln Park. There is also one variant that is both haemoglobin Lepore and haemoglobin Anti-Lepore (HbParchman). Compare: haemoglobin Lepore. (05 Mar 2000) |
| haemoglobin Lepore | A group of abnormal Hb's with normal a chains, but the non-a chains consist of the N-terminal portion of the d chain joined to the C-terminal portion of the b chain, apparently as the result of nonhomologous pairing and crossing over between the genes for b and d chains. The major types are Hb LeporeBoston (identical to Hb LeporeWashington), Hb LeporeHollandia, and Hb LeporeBaltimore, which differ in the region of crossing over (d87-b116, d22-b50, and d50-b86, respectively). Heterozygotes form about 10% Hb Lepore, normal amounts of Hb A2, and moderately increased amounts of Hb F and usually have mild anaemia, microcytosis, and hypochromia; homozygotes form only Hb Lepore and Hb F and have severe anaemia. Compare: haemoglobin Anti-Lepore. (05 Mar 2000) |
| Lepore haemoglobin | <haematology> Variant haemoglobin in a rare form of thalassaemia: there is a composite _ _ chain as a result of an unequal crossing over event. The composite chain is functional but synthesised at reduced rate. (18 Nov 1997) |
| Lepore thalassaemia | Thalassaemia syndrome due to production of abnormally structured Lepore haemoglobin. Heterozygous state: thalassaemia minor with about 10% of Hb Lepore, Hb F moderately increased, Hb A2 normal. Homozygous state: thalassaemia major with only Hb F and Hb Lepore produced, no Hb A or Hb A2. (05 Mar 2000) |
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